|
Name |
Accession |
Description |
Interval |
E-value |
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
16-584 |
9.30e-169 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 492.37 E-value: 9.30e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 16 WRQLISSVGSQARMLRRSMLALLLAAFMQGIAFACLYPIIDALLRG-DAPQLLNWAMAFSVAAIVTLVLRWYGLgfeYRG 94
Cdd:COG1132 9 LRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGgDLSALLLLLLLLLGLALLRALLSYLQR---YLL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 95 HLA--QATHELRLRLGEQLRRVPLEKLQRGRAGEMNALLLGSVDENLNYVIAIANILLLTIVTPLTASLATLWIDWRLGL 172
Cdd:COG1132 86 ARLaqRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWRLAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 173 VMLLIFPLLVPFYYWRRPAMRRQMQTLGEAHQRLSGDIVEFAQGMMVLRTCGSDADKSRALLAHFNALENLQTRTHRQGA 252
Cdd:COG1132 166 IVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARLSA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 253 GATMLIASVVELGLQVVVLSGIVWVVTGTLNLAFLIAAVAMIMRFAEPMAMFISYTSVVELIASALQRIERFMAIAPL-- 330
Cdd:COG1132 246 LFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPPEip 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 331 -PVAEQSEMPERYDIRFDNVSYRYEEGDgHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDI 409
Cdd:COG1132 326 dPPGAVPLPPVRGEIEFENVSFSYPGDR-PVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDI 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 410 RRLTPEQLNSLISVVFQDVWLFDDTLLANIRIARPQATRQEVEEAARAAQCLEFISRLPQGWLTPMGEMGGQLSGGERQR 489
Cdd:COG1132 405 RDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQR 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 490 ISIARALLKNAPVVILDEPTAALDIESELAVQKAIDNLVHNRTVIIIAHRLSTIAGAGNILVIEEGQVVEQGTHAQLLSH 569
Cdd:COG1132 485 IAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELLAR 564
|
570
....*....|....*
gi 1805558896 570 HGRYQALWQAQMAAR 584
Cdd:COG1132 565 GGLYARLYRLQFGEE 579
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
13-581 |
1.62e-123 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 380.72 E-value: 1.62e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 13 RVNWRQLISSVGSQARMLRRSMLALLLAAFMqGIAFACLYP-IIDALLRGDAPQLLNW-AMAFSVAAIVTLVLRWYglgf 90
Cdd:COG2274 141 PFGLRWFLRLLRRYRRLLLQVLLASLLINLL-ALATPLFTQvVIDRVLPNQDLSTLWVlAIGLLLALLFEGLLRLL---- 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 91 eyRGHL-----AQATHELRLRLGEQLRRVPLEKLQRGRAGEmnalLLGSVDENLNYVIAIANILLLTIVTPLTA--SLAT 163
Cdd:COG2274 216 --RSYLllrlgQRIDLRLSSRFFRHLLRLPLSFFESRSVGD----LASRFRDVESIREFLTGSLLTALLDLLFVliFLIV 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 164 LW-IDWRLGLVMLLIFPLLVPFYYWRRPAMRRQMQTLGEAHQRLSGDIVEFAQGMMVLRTCGSDADKSRALLAHFNALEN 242
Cdd:COG2274 290 LFfYSPPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRWENLLAKYLN 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 243 LQTRTHRQGAGATMLIASVVELGLQVVVLSGIVWVVTGTLNLAFLIAAVAMIMRFAEPMAMFISYTSVVELIASALQRIE 322
Cdd:COG2274 370 ARFKLRRLSNLLSTLSGLLQQLATVALLWLGAYLVIDGQLTLGQLIAFNILSGRFLAPVAQLIGLLQRFQDAKIALERLD 449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 323 RFMAIAPLPVAEQSEMP---ERYDIRFDNVSYRYEEGDGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQ 399
Cdd:COG2274 450 DILDLPPEREEGRSKLSlprLKGDIELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTS 529
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 400 GQISIGGVDIRRLTPEQLNSLISVVFQDVWLFDDTLLANIRIARPQATRQEVEEAARAAQCLEFISRLPQGWLTPMGEMG 479
Cdd:COG2274 530 GRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGG 609
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 480 GQLSGGERQRISIARALLKNAPVVILDEPTAALDIESELAVQKAIDNLVHNRTVIIIAHRLSTIAGAGNILVIEEGQVVE 559
Cdd:COG2274 610 SNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVE 689
|
570 580
....*....|....*....|..
gi 1805558896 560 QGTHAQLLSHHGRYQALWQAQM 581
Cdd:COG2274 690 DGTHEELLARKGLYAELVQQQL 711
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
102-578 |
1.04e-113 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 350.61 E-value: 1.04e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 102 ELRLRLGEQLRRVPLEKLQRGRAGEMNALLLGSVDenlnyviAIANILLLTIVTPLTASLATL-------WIDWRLGLVM 174
Cdd:COG4987 89 DLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADVD-------ALDNLYLRVLLPLLVALLVILaavaflaFFSPALALVL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 175 ---LLIFPLLVPFYYWRrpAMRRQMQTLGEAHQRLSGDIVEFAQGMMVLRTCGSDADKSRALLAHFNALENLQTRTHRQG 251
Cdd:COG4987 162 algLLLAGLLLPLLAAR--LGRRAGRRLAAARAALRARLTDLLQGAAELAAYGALDRALARLDAAEARLAAAQRRLARLS 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 252 AGATMLIASVVELGLQVVVLSGIVWVVTGTLNLAFLIAAVAMIMRFAEPMAMFISytsVVELIASALQRIERFMAIAPLP 331
Cdd:COG4987 240 ALAQALLQLAAGLAVVAVLWLAAPLVAAGALSGPLLALLVLAALALFEALAPLPA---AAQHLGRVRAAARRLNELLDAP 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 332 VA-----EQSEMPERYDIRFDNVSYRYEEGDGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGG 406
Cdd:COG4987 317 PAvtepaEPAPAPGGPSLELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGG 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 407 VDIRRLTPEQLNSLISVVFQDVWLFDDTLLANIRIARPQATRQEVEEAARAAQCLEFISRLPQGWLTPMGEMGGQLSGGE 486
Cdd:COG4987 397 VDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGE 476
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 487 RQRISIARALLKNAPVVILDEPTAALDIESELAVQKAIDNLVHNRTVIIIAHRLSTIAGAGNILVIEEGQVVEQGTHAQL 566
Cdd:COG4987 477 RRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEEL 556
|
490
....*....|..
gi 1805558896 567 LSHHGRYQALWQ 578
Cdd:COG4987 557 LAQNGRYRQLYQ 568
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
17-571 |
2.25e-113 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 349.83 E-value: 2.25e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 17 RQLISSVGSQARMLRRSMLALLLAAFMqGIAFA-CLYPIIDALLRGDAP--QLLNWAMAFSVAAIVTLVLRWyglGFEYR 93
Cdd:COG4988 6 KRLKRLARGARRWLALAVLLGLLSGLL-IIAQAwLLASLLAGLIIGGAPlsALLPLLGLLLAVLLLRALLAW---LRERA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 94 GHLA--QATHELRLRLGEQLRRVPLEKLQRGRAGEMNALLLGSVDENLNYVIAIANILLLTIVTPLTASLATLWIDWRLG 171
Cdd:COG4988 82 AFRAaaRVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLTEGVEALDGYFARYLPQLFLAALVPLLILVAVFPLDWLSG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 172 LVMLLIFPLlVPFYYW-----RRPAMRRQMQTLgeahQRLSGDIVEFAQGMMVLRTCGSDADKSRALlahfnaleNLQTR 246
Cdd:COG4988 162 LILLVTAPL-IPLFMIlvgkgAAKASRRQWRAL----ARLSGHFLDRLRGLTTLKLFGRAKAEAERI--------AEASE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 247 THRQgagATM-------LIASVVE----LGLQVVVLSGIVWVVTGTLNLAFLIAAVAMIMRFAEPMAMFISYTSVVELIA 315
Cdd:COG4988 229 DFRK---RTMkvlrvafLSSAVLEffasLSIALVAVYIGFRLLGGSLTLFAALFVLLLAPEFFLPLRDLGSFYHARANGI 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 316 SALQRIERFMAiAPLPVAEQSE----MPERYDIRFDNVSYRYEEGdGHALNHVSLTFPAASMSALVGASGAGKTTVTKLL 391
Cdd:COG4988 306 AAAEKIFALLD-APEPAAPAGTaplpAAGPPSIELEDVSFSYPGG-RPALDGLSLTIPPGERVALVGPSGAGKSTLLNLL 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 392 MRYADPQQGQISIGGVDIRRLTPEQLNSLISVVFQDVWLFDDTLLANIRIARPQATRQEVEEAARAAQCLEFISRLPQGW 471
Cdd:COG4988 384 LGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEAALEAAGLDEFVAALPDGL 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 472 LTPMGEMGGQLSGGERQRISIARALLKNAPVVILDEPTAALDIESELAVQKAIDNLVHNRTVIIIAHRLSTIAGAGNILV 551
Cdd:COG4988 464 DTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQADRILV 543
|
570 580
....*....|....*....|
gi 1805558896 552 IEEGQVVEQGTHAQLLSHHG 571
Cdd:COG4988 544 LDDGRIVEQGTHEELLAKNG 563
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
344-577 |
8.84e-106 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 318.41 E-value: 8.84e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 344 IRFDNVSYRYEEGDGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLTPEQLNSLISV 423
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 424 VFQDVWLFDDTLLANIRIARPQATRQEVEEAARAAQCLEFISRLPQGWLTPMGEMGGQLSGGERQRISIARALLKNAPVV 503
Cdd:cd03251 81 VSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1805558896 504 ILDEPTAALDIESELAVQKAIDNLVHNRTVIIIAHRLSTIAGAGNILVIEEGQVVEQGTHAQLLSHHGRYQALW 577
Cdd:cd03251 161 ILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKLH 234
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
16-582 |
1.65e-101 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 319.35 E-value: 1.65e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 16 WRQLISSVGSQARMLRRSMLALLLAAFMQGIAFACLYPIIDALLRGDAPQLLnWAMAfsvAAIVTLVLrWYGLGfEYRGH 95
Cdd:TIGR02203 2 FRRLWSYVRPYKAGLVLAGVAMILVAATESTLAALLKPLLDDGFGGRDRSVL-WWVP---LVVIGLAV-LRGIC-SFVST 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 96 LAQA------THELRLRLGEQLRRVPLEKLQRGRAGEMNALLLGSVDENLNYVIAIANILLLTIVTPLTASLATLWIDWR 169
Cdd:TIGR02203 76 YLLSwvsnkvVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYYSWQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 170 LGLVMLLIFPLLVpfyyWRRPAMRRQMQTLGEAHQRLSGD----IVEFAQGMMVLRTCGSDADKSRALLAHFNALENLQT 245
Cdd:TIGR02203 156 LTLIVVVMLPVLS----ILMRRVSKRLRRISKEIQNSMGQvttvAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRRLAM 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 246 RTHRQGAGATMLIASVVELGLQVVVLSGIVWVVTGTLN----LAFLIAAVAMImrfaEPMAMFISYTSVVELIASALQRI 321
Cdd:TIGR02203 232 KMTSAGSISSPITQLIASLALAVVLFIALFQAQAGSLTagdfTAFITAMIALI----RPLKSLTNVNAPMQRGLAAAESL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 322 ERFMAIAPLPVAEQSEMPE-RYDIRFDNVSYRYEEGDGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQG 400
Cdd:TIGR02203 308 FTLLDSPPEKDTGTRAIERaRGDVEFRNVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSG 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 401 QISIGGVDIRRLTPEQLNSLISVVFQDVWLFDDTLLANIRIARP-QATRQEVEEAARAAQCLEFISRLPQGWLTPMGEMG 479
Cdd:TIGR02203 388 QILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRTeQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENG 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 480 GQLSGGERQRISIARALLKNAPVVILDEPTAALDIESELAVQKAIDNLVHNRTVIIIAHRLSTIAGAGNILVIEEGQVVE 559
Cdd:TIGR02203 468 VLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVE 547
|
570 580
....*....|....*....|...
gi 1805558896 560 QGTHAQLLSHHGRYQALWQAQMA 582
Cdd:TIGR02203 548 RGTHNELLARNGLYAQLHNMQFR 570
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
1-584 |
4.93e-101 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 319.07 E-value: 4.93e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 1 MKDNNPADNLAWRVNWRQLISSVGSQARMLRRSMLALLLAAFmqGIAFACLYPIIDALLRGDAPQLLNWAMAFSVAAIVT 80
Cdd:COG5265 6 AMSAPAAPPRLDLLLRLLLLLLLPPYLRRRRRALAALLLLLL--AAALALVVPPLLKDAIDALLSGAAALLVVPVGLLLA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 81 L-VLRWYGLGF-EYR----GHLAQ-ATHELRLRLGEQLRRVPLE-KLQRgRAGEMNALL---LGSVDENLNYviaianiL 149
Cdd:COG5265 84 YgLLRLLSVLFgELRdalfARVTQrAVRRLALEVFRHLHALSLRfHLER-QTGGLSRDIergTKGIEFLLRF-------L 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 150 LLTIVtP----LTASLATLWI--DWRLGLVMLLIFPLLVPFYYW---RRPAMRRQMQTL-GEAHQR-----LSGDIVEF- 213
Cdd:COG5265 156 LFNIL-PtlleIALVAGILLVkyDWWFALITLVTVVLYIAFTVVvteWRTKFRREMNEAdSEANTRavdslLNYETVKYf 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 214 -AQGMMVLRtcgsdADKSRAllahfnALENLQTRTHRQ----GAGATMLIAsvveLGLQVVVLSGIVWVVTGTLNLAFLI 288
Cdd:COG5265 235 gNEAREARR-----YDEALA------RYERAAVKSQTSlallNFGQALIIA----LGLTAMMLMAAQGVVAGTMTVGDFV 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 289 AAVAMIMRFAEPMaMFISYtsVVELIASALQRIERFMAIaplpVAEQSEMPERYD----------IRFDNVSYRYEeGDG 358
Cdd:COG5265 300 LVNAYLIQLYIPL-NFLGF--VYREIRQALADMERMFDL----LDQPPEVADAPDapplvvgggeVRFENVSFGYD-PER 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 359 HALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLTPEQLNSLISVVFQDVWLFDDTLLAN 438
Cdd:COG5265 372 PILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYN 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 439 IRIARPQATRQEVEEAARAAQCLEFISRLPQGWLTPMGEMGGQLSGGERQRISIARALLKNAPVVILDEPTAALDIESEL 518
Cdd:COG5265 452 IAYGRPDASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTER 531
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1805558896 519 AVQKAIDNLVHNRTVIIIAHRLSTIAGAGNILVIEEGQVVEQGTHAQLLSHHGRYQALWQAQMAAR 584
Cdd:COG5265 532 AIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQMWARQQEEE 597
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
344-580 |
2.91e-97 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 296.45 E-value: 2.91e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 344 IRFDNVSYRYEEGdGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLTPEQLNSLISV 423
Cdd:cd03253 1 IEFENVTFAYDPG-RPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 424 VFQDVWLFDDTLLANIRIARPQATRQEVEEAARAAQCLEFISRLPQGWLTPMGEMGGQLSGGERQRISIARALLKNAPVV 503
Cdd:cd03253 80 VPQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPIL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1805558896 504 ILDEPTAALDIESELAVQKAIDNLVHNRTVIIIAHRLSTIAGAGNILVIEEGQVVEQGTHAQLLSHHGRYQALWQAQ 580
Cdd:cd03253 160 LLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKAQ 236
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
344-580 |
4.88e-97 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 295.99 E-value: 4.88e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 344 IRFDNVSYRYEEGDGH-ALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLTPEQLNSLIS 422
Cdd:cd03249 1 IEFKNVSFRYPSRPDVpILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 423 VVFQDVWLFDDTLLANIRIARPQATRQEVEEAARAAQCLEFISRLPQGWLTPMGEMGGQLSGGERQRISIARALLKNAPV 502
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1805558896 503 VILDEPTAALDIESELAVQKAIDNLVHNRTVIIIAHRLSTIAGAGNILVIEEGQVVEQGTHAQLLSHHGRYQALWQAQ 580
Cdd:cd03249 161 LLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
343-571 |
1.23e-91 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 281.81 E-value: 1.23e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 343 DIRFDNVSYRYEEGDgHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLTPEQLNSLIS 422
Cdd:cd03254 2 EIEFENVNFSYDEKK-PVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 423 VVFQDVWLFDDTLLANIRIARPQATRQEVEEAARAAQCLEFISRLPQGWLTPMGEMGGQLSGGERQRISIARALLKNAPV 502
Cdd:cd03254 81 VVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1805558896 503 VILDEPTAALDIESELAVQKAIDNLVHNRTVIIIAHRLSTIAGAGNILVIEEGQVVEQGTHAQLLSHHG 571
Cdd:cd03254 161 LILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
35-596 |
1.96e-87 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 283.01 E-value: 1.96e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 35 LALLLAAFMQGIAFAclyPIIDALLRGDA--PQLLNWAmAFSVAAIVTLVL-----------RWYGLGFEYRGHLAQ--- 98
Cdd:PRK13657 29 VLLAAATFAEPILFG---RIIDAISGKGDifPLLAAWA-GFGLFNIIAGVLvarhadrlahrRRLAVLTEYFERIIQlpl 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 99 ----ATHELRLrlgeqlrrvpLEKLQRGRAGeMNALLLGSVDENLnyviaiANILLLTIVTPLTaslatLWIDWRLGLVM 174
Cdd:PRK13657 105 awhsQRGSGRA----------LHTLLRGTDA-LFGLWLEFMREHL------ATLVALVVLLPLA-----LFMNWRLSLVL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 175 LLifpLLVPFYYWRRPAMRR--QMQTLGEAHQR-LSGDIVEFAQGMMVLRTCGSDADKSRALLAHFNALENLQTRTHRQG 251
Cdd:PRK13657 163 VV---LGIVYTLITTLVMRKtkDGQAAVEEHYHdLFAHVSDAIGNVSVVQSYNRIEAETQALRDIADNLLAAQMPVLSWW 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 252 AGATMLIASVVELGLQVVVLSGIVWVVTGTLNlaflIAAVAMIMRFAEpmaMFIS----YTSVVELIASALQRIERFMAI 327
Cdd:PRK13657 240 ALASVLNRAASTITMLAILVLGAALVQKGQLR----VGEVVAFVGFAT---LLIGrldqVVAFINQVFMAAPKLEEFFEV 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 328 --APLPVAEQSEMPE----RYDIRFDNVSYRYEeGDGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQ 401
Cdd:PRK13657 313 edAVPDVRDPPGAIDlgrvKGAVEFDDVSFSYD-NSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGR 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 402 ISIGGVDIRRLTPEQLNSLISVVFQDVWLFDDTLLANIRIARPQATRQEVEEAARAAQCLEFISRLPQGWLTPMGEMGGQ 481
Cdd:PRK13657 392 ILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQ 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 482 LSGGERQRISIARALLKNAPVVILDEPTAALDIESELAVQKAIDNLVHNRTVIIIAHRLSTIAGAGNILVIEEGQVVEQG 561
Cdd:PRK13657 472 LSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESG 551
|
570 580 590
....*....|....*....|....*....|....*.
gi 1805558896 562 THAQLLSHHGRYQALWQAQ-MAARVWRDDGVSASGE 596
Cdd:PRK13657 552 SFDELVARGGRFAALLRAQgMLQEDERRKQPAAEGA 587
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
343-580 |
4.14e-87 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 281.91 E-value: 4.14e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 343 DIRFDNVSYRYEEGDGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLTPEQLNSLIS 422
Cdd:PRK11176 341 DIEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVA 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 423 VVFQDVWLFDDTLLANIRIARP-QATRQEVEEAARAAQCLEFISRLPQGWLTPMGEMGGQLSGGERQRISIARALLKNAP 501
Cdd:PRK11176 421 LVSQNVHLFNDTIANNIAYARTeQYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSP 500
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1805558896 502 VVILDEPTAALDIESELAVQKAIDNLVHNRTVIIIAHRLSTIAGAGNILVIEEGQVVEQGTHAQLLSHHGRYQALWQAQ 580
Cdd:PRK11176 501 ILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNGVYAQLHKMQ 579
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
54-580 |
2.42e-81 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 266.57 E-value: 2.42e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 54 IIDALLRGDAPQLLNwaMAFSVAAIVTLVLrwyGLGFEYRGHLAQATHE-----LRLRLGEQLRRVPLEKLQRGRAGEMN 128
Cdd:TIGR02204 44 MIDHGFSKDSSGLLN--RYFAFLLVVALVL---ALGTAARFYLVTWLGErvvadIRRAVFAHLISLSPSFFDKNRSGEVV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 129 ALLLGSVDENLNYVIAIANILLLTIVTPLTASLATLWIDWRLGLVMLLIFPL-LVPFYywrrpAMRRQMQTLGEAHQRLS 207
Cdd:TIGR02204 119 SRLTTDTTLLQSVIGSSLSMALRNALMCIGGLIMMFITSPKLTSLVLLAVPLvLLPIL-----LFGRRVRKLSRESQDRI 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 208 GDIVEFA-QGMMVLRTC----GSDADKSRALLAHFNALENLQTRTHRQgagaTMLIASVVELGLQVVVlsGIVWVvTGTL 282
Cdd:TIGR02204 194 ADAGSYAgETLGAIRTVqafgHEDAERSRFGGAVEKAYEAARQRIRTR----ALLTAIVIVLVFGAIV--GVLWV-GAHD 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 283 NLAFLIAA--VAMIMRFAEPMAMFISYTSVV--EL--IASALQRIERFM----AIAPLPVAEQSEMPERYDIRFDNVSYR 352
Cdd:TIGR02204 267 VIAGKMSAgtLGQFVFYAVMVAGSIGTLSEVwgELqrAAGAAERLIELLqaepDIKAPAHPKTLPVPLRGEIEFEQVNFA 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 353 Y-EEGDGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLTPEQLNSLISVVFQDVWLF 431
Cdd:TIGR02204 347 YpARPDQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDPAELRARMALVPQDPVLF 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 432 DDTLLANIRIARPQATRQEVEEAARAAQCLEFISRLPQGWLTPMGEMGGQLSGGERQRISIARALLKNAPVVILDEPTAA 511
Cdd:TIGR02204 427 AASVMENIRYGRPDATDEEVEAAARAAHAHEFISALPEGYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSA 506
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1805558896 512 LDIESELAVQKAIDNLVHNRTVIIIAHRLSTIAGAGNILVIEEGQVVEQGTHAQLLSHHGRYQALWQAQ 580
Cdd:TIGR02204 507 LDAESEQLVQQALETLMKGRTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELIAKGGLYARLARLQ 575
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
26-552 |
4.17e-79 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 259.53 E-value: 4.17e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 26 QARMLRRSM-LALLLAAFMQGIAFACLYPIIDALLRGDAPQ-LLNWAMAFSVAAIVTLVLRWYGLGFEYRGHLAqATHEL 103
Cdd:TIGR02857 1 ARRALALLAlLGVLGALLIIAQAWLLARVVDGLISAGEPLAeLLPALGALALVLLLRALLGWLQERAAARAAAA-VKSQL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 104 RLRLGEQLRRVPLEKLQRGRAGEMNALLLGSVDENLNYVIAIANILLLTIVTPLTASLATLWIDWRLGLVMLLIFPLlVP 183
Cdd:TIGR02857 80 RERLLEAVAALGPRWLQGRPSGELATLALEGVEALDGYFARYLPQLVLAVIVPLAILAAVFPQDWISGLILLLTAPL-IP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 184 FYYW-----RRPAMRRQMQTLgeahQRLSGDIVEFAQGMMVLRTCGSdADKSRALLAHfnALENLQTRTHR-------QG 251
Cdd:TIGR02857 159 IFMIligwaAQAAARKQWAAL----SRLSGHFLDRLRGLPTLKLFGR-AKAQAAAIRR--SSEEYRERTMRvlriaflSS 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 252 AG----ATMLIASV-VELGLQVVVlsgivwvvtGTLNLAFLIAAVAMIMRFAEPMAMF-ISYTSVVELIAsALQRIERFM 325
Cdd:TIGR02857 232 AVlelfATLSVALVaVYIGFRLLA---------GDLDLATGLFVLLLAPEFYLPLRQLgAQYHARADGVA-AAEALFAVL 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 326 AIAPLPVAEQSEMPERYD--IRFDNVSYRYEeGDGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQIS 403
Cdd:TIGR02857 302 DAAPRPLAGKAPVTAAPAssLEFSGVSVAYP-GRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIA 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 404 IGGVDIRRLTPEQLNSLISVVFQDVWLFDDTLLANIRIARPQATRQEVEEAARAAQCLEFISRLPQGWLTPMGEMGGQLS 483
Cdd:TIGR02857 381 VNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLS 460
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1805558896 484 GGERQRISIARALLKNAPVVILDEPTAALDIESELAVQKAIDNLVHNRTVIIIAHRLSTIAGAGNILVI 552
Cdd:TIGR02857 461 GGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
344-556 |
7.29e-75 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 236.13 E-value: 7.29e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 344 IRFDNVSYRYEEGDGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLTPEQLNSLISV 423
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 424 VFQDVWLFDDTLLANIriarpqatrqeveeaaraaqclefisrlpqgwltpmgemggqLSGGERQRISIARALLKNAPVV 503
Cdd:cd03228 81 VPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPPIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1805558896 504 ILDEPTAALDIESELAVQKAIDNLVHNRTVIIIAHRLSTIAGAGNILVIEEGQ 556
Cdd:cd03228 119 ILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
344-580 |
2.96e-70 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 226.60 E-value: 2.96e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 344 IRFDNVSYRYEEGDGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLTPEQLNSLISV 423
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 424 VFQDVWLFDDTLLANIRIARPQATRQEVEEAARAAQCLEFISRLPQGWLTPMGEMGGQLSGGERQRISIARALLKNAPVV 503
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1805558896 504 ILDEPTAALDIESELAVQKAIDNLVHNRTVIIIAHRLSTIAGAGNILVIEEGQVVEQGTHAQLLSHHGRYQALWQAQ 580
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQLQ 237
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
54-579 |
5.60e-69 |
|
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein in bacteria. It belongs to the larger ABC transporter superfamily with the characteristic ATP binding motif. The In general, this protein is in some ways implicated in osmoregulation and suggested to participate in the export of glucan from the cytoplasm to periplasm. The cyclic beta-1,2-glucan in the bactrerial periplasmic space is suggested to confer the property of high osmolority. It has also been demonstrated that mutants in this loci have lost functions of virulence and motility. It is unclear as to how virulence and osmoadaptaion are related. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 130260 [Multi-domain] Cd Length: 585 Bit Score: 234.01 E-value: 5.60e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 54 IIDALLRGD--APQLLNWaMAFSVAAIVTLVLrwYGLGFEYRGHLAQAThelrlRLGEQLRRV---PLE-KLQRGRAGEM 127
Cdd:TIGR01192 45 IIDAISSKSdvLPTLALW-AGFGVFNTIAYVL--VAREADRLAHGRRAT-----LLTEAFGRIismPLSwHQQRGTSNAL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 128 NALLLGSvDENLNYVIAIANILLLTIVTPLTASLATLWIDWRLGLVMLLIFPLLVPFYYWRRPAMRRQMQTLGEAHQRLS 207
Cdd:TIGR01192 117 HTLLRAT-ETLFGLWLEFMRQHLATFVALFLLIPTAFAMDWRLSIVLMVLGILYILIAKLVMQRTKNGQAAVEHHYHNVF 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 208 GDIVEFAQGMMVLRTCGSDADKSRALLAHFNALENLQTRTHRQGAGATMLIASVVELGLQVVVLSGIVWVVTGTLNLAFL 287
Cdd:TIGR01192 196 KHVSDSISNVSVVHSYNRIEAETSALKQFTNNLLSAQYPVLDWWALASGLNRMASTISMMCILVIGTVLVIKGELSVGEV 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 288 IAAVA----MIMRFaEPMAMFISytsvveLIASALQRIERF--MAIAPLPVAEQSEMPE----RYDIRFDNVSYRYEEgD 357
Cdd:TIGR01192 276 IAFIGfanlLIGRL-DQMSGFIT------QIFEARAKLEDFfdLEDSVFQREEPADAPElpnvKGAVEFRHITFEFAN-S 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 358 GHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLTPEQLNSLISVVFQDVWLFDDTLLA 437
Cdd:TIGR01192 348 SQGVFDVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQILIDGIDINTVTRESLRKSIATVFQDAGLFNRSIRE 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 438 NIRIARPQATRQEVEEAARAAQCLEFISRLPQGWLTPMGEMGGQLSGGERQRISIARALLKNAPVVILDEPTAALDIESE 517
Cdd:TIGR01192 428 NIRLGREGATDEEVYEAAKAAAAHDFILKRSNGYDTLVGERGNRLSGGERQRLAIARAILKNAPILVLDEATSALDVETE 507
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1805558896 518 LAVQKAIDNLVHNRTVIIIAHRLSTIAGAGNILVIEEGQVVEQGTHAQLLSHHGRYQALWQA 579
Cdd:TIGR01192 508 ARVKNAIDALRKNRTTFIIAHRLSTVRNADLVLFLDQGRLIEKGSFQELIQKDGRFYKLLRR 569
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
149-578 |
2.49e-65 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 223.93 E-value: 2.49e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 149 LLLTIVTPLTASLATL--------WIDWRLG-------LVMLLIFPLLvpFYYWRRPAMRRQMQTLGEAHQRLsgdiVEF 213
Cdd:PRK11160 133 LYLRLISPLVAALVVIlvltiglsFFDLTLAltlggilLLLLLLLPLL--FYRLGKKPGQDLTHLRAQYRVQL----TEW 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 214 AQGMMVLRTCGSdADKSRALLAhfNALENLQTRTHRQG-----AGATMLIASvvelGLQVVVlsgIVWVVTGTLN----- 283
Cdd:PRK11160 207 LQGQAELTLFGA-EDRYRQQLE--QTEQQWLAAQRRQAnltglSQALMILAN----GLTVVL---MLWLAAGGVGgnaqp 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 284 ------LAFLI-AAVAMIMrfaePMAMFISYTSVVelIASAlQRIERFMAIAPLPV--AEQSEMPERYDIRFDNVSYRYE 354
Cdd:PRK11160 277 galialFVFAAlAAFEALM----PVAGAFQHLGQV--IASA-RRINEITEQKPEVTfpTTSTAAADQVSLTLNNVSFTYP 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 355 EGDGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLTPEQLNSLISVVFQDVWLFDDT 434
Cdd:PRK11160 350 DQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSAT 429
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 435 LLANIRIARPQATRQEVEEAARAAQcLEFISRLPQGWLTPMGEMGGQLSGGERQRISIARALLKNAPVVILDEPTAALDI 514
Cdd:PRK11160 430 LRDNLLLAAPNASDEALIEVLQQVG-LEKLLEDDKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDA 508
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1805558896 515 ESElavQKAIDNLVH---NRTVIIIAHRLSTIAGAGNILVIEEGQVVEQGTHAQLLSHHGRYQALWQ 578
Cdd:PRK11160 509 ETE---RQILELLAEhaqNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGRYYQLKQ 572
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
343-562 |
3.42e-61 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 202.34 E-value: 3.42e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 343 DIRFDNVSYRYEEGDGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLTPEQLNSLIS 422
Cdd:cd03244 2 DIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 423 VVFQDVWLFDDTLLANIRiarP--QATRQEVEEAARAAQCLEFISRLPQGWLTPMGEMGGQLSGGERQRISIARALLKNA 500
Cdd:cd03244 82 IIPQDPVLFSGTIRSNLD---PfgEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1805558896 501 PVVILDEPTAALDIESELAVQKAIDNLVHNRTVIIIAHRLSTIAGAGNILVIEEGQVVEQGT 562
Cdd:cd03244 159 KILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
65-580 |
6.82e-61 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 211.88 E-value: 6.82e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 65 QLLNWAMAFSVAAIVTLVLR--WYGLGFEYRGHLAQathELRLRLGEQLRRVPLEKLQRGRAGEMNALLLGSVDEnlnyV 142
Cdd:PRK10789 34 QILMWIGTMVLIAVVVYLLRyvWRVLLFGASYQLAV---ELREDFYRQLSRQHPEFYLRHRTGDLMARATNDVDR----V 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 143 IAIANILLLTIVTPLTASLATL-----WIDWRLGLVMLLIFPLLVPfyywrrpAMRRQMQTLgeaHQRLsgdivEFAQGm 217
Cdd:PRK10789 107 VFAAGEGVLTLVDSLVMGCAVLivmstQISWQLTLLALLPMPVMAI-------MIKRYGDQL---HERF-----KLAQA- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 218 mVLRTCGSDADKSRALLAHFNA--LENLQTRTHRQGAGAT----MLIASV---------VELGL-QVVVLSGIVW-VVTG 280
Cdd:PRK10789 171 -AFSSLNDRTQESLTSIRMIKAfgLEDRQSALFAADAEDTgkknMRVARIdarfdptiyIAIGMaNLLAIGGGSWmVVNG 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 281 TLNLAFLIAAVAMIMRFAEPMAMFISYTSVVELIASALQRIERFMAIAPLPV-AEQSEMPERYDIRFDNVSYRYEEGDGH 359
Cdd:PRK10789 250 SLTLGQLTSFVMYLGLMIWPMLALAWMFNIVERGSAAYSRIRAMLAEAPVVKdGSEPVPEGRGELDVNIRQFTYPQTDHP 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 360 ALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLTPEQLNSLISVVFQDVWLFDDTLLANI 439
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNI 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 440 RIARPQATRQEVEEAARAAQCLEFISRLPQGWLTPMGEMGGQLSGGERQRISIARALLKNAPVVILDEPTAALDIESELA 519
Cdd:PRK10789 410 ALGRPDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQ 489
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1805558896 520 VQKAIDNLVHNRTVIIIAHRLSTIAGAGNILVIEEGQVVEQGTHAQLLSHHGRYQALWQAQ 580
Cdd:PRK10789 490 ILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWYRDMYRYQ 550
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
144-576 |
8.27e-61 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 214.60 E-value: 8.27e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 144 AIANILL-----LTIVtpLTASLATLWIDWRLGLVMLLIFPLLVPFYYWRRPAMRRQMQTLGEAHQRLSGDIVEFAQGMM 218
Cdd:TIGR01193 268 ALASTILslfldMWIL--VIVGLFLVRQNMLLFLLSLLSIPVYAVIIILFKRTFNKLNHDAMQANAVLNSSIIEDLNGIE 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 219 VLRTCGSDADKSRALLAHFNALENLQTRTHRQGAGaTMLIASVVELGLQVVVL-SGIVWVVTGTLNLAFLIAAVAMIMRF 297
Cdd:TIGR01193 346 TIKSLTSEAERYSKIDSEFGDYLNKSFKYQKADQG-QQAIKAVTKLILNVVILwTGAYLVMRGKLTLGQLITFNALLSYF 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 298 AEPMAMFISYTSVVELIASALQRIERFMaIAPLPVAEQSEMPER----YDIRFDNVSYRYEEGDgHALNHVSLTFPAASM 373
Cdd:TIGR01193 425 LTPLENIINLQPKLQAARVANNRLNEVY-LVDSEFINKKKRTELnnlnGDIVINDVSYSYGYGS-NILSDISLTIKMNSK 502
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 374 SALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLTPEQLNSLISVVFQDVWLFDDTLLANIRI-ARPQATRQEVE 452
Cdd:TIGR01193 503 TTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLgAKENVSQDEIW 582
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 453 EAARAAQCLEFISRLPQGWLTPMGEMGGQLSGGERQRISIARALLKNAPVVILDEPTAALDIESElavQKAIDNLV--HN 530
Cdd:TIGR01193 583 AACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITE---KKIVNNLLnlQD 659
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1805558896 531 RTVIIIAHRLSTIAGAGNILVIEEGQVVEQGTHAQLLSHHGRYQAL 576
Cdd:TIGR01193 660 KTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASL 705
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
343-561 |
2.51e-60 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 199.74 E-value: 2.51e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 343 DIRFDNVSYRYEEGDGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLTPEQLNSLIS 422
Cdd:cd03245 2 RIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 423 VVFQDVWLFDDTLLANIRIARPQATRQEVEEAARAAQCLEFISRLPQGWLTPMGEMGGQLSGGERQRISIARALLKNAPV 502
Cdd:cd03245 82 YVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPPI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1805558896 503 VILDEPTAALDIESELAVQKAIDNLVHNRTVIIIAHRLSTIAGAGNILVIEEGQVVEQG 561
Cdd:cd03245 162 LLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
102-540 |
2.11e-59 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 206.83 E-value: 2.11e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 102 ELRLRLGEQLRRVPLEKLQRGRAGEMNALLLGSVDENLNYVIAIANILLLTIVTPLTASLATLWIDWRLGLVM---LLIF 178
Cdd:TIGR02868 87 ALRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQDLYVRVIVPAGVALVVGAAAVAAIAVLSVPAALILaagLLLA 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 179 PLLVPFYYWRrpAMRRQMQTLGEAHQRLSGDIVEFAQGMMVLRTCGSDAD---KSRALLAHFNALENLQTRTHRQGAGAT 255
Cdd:TIGR02868 167 GFVAPLVSLR--AARAAEQALARLRGELAAQLTDALDGAAELVASGALPAalaQVEEADRELTRAERRAAAATALGAALT 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 256 MLIASVVELGlqvVVLSGIVWVVTGTLNLAFLIAAVAMIMRFAEPMAMFISYTSVVELIASALQRIERFMAiAPLPVAEQ 335
Cdd:TIGR02868 245 LLAAGLAVLG---ALWAGGPAVADGRLAPVTLAVLVLLPLAAFEAFAALPAAAQQLTRVRAAAERIVEVLD-AAGPVAEG 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 336 S------EMPERYDIRFDNVSYRYEeGDGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDI 409
Cdd:TIGR02868 321 SapaagaVGLGKPTLELRDLSAGYP-GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPV 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 410 RRLTPEQLNSLISVVFQDVWLFDDTLLANIRIARPQATRQEVEEAARAAQCLEFISRLPQGWLTPMGEMGGQLSGGERQR 489
Cdd:TIGR02868 400 SSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQR 479
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1805558896 490 ISIARALLKNAPVVILDEPTAALDIESELAVQKAIDNLVHNRTVIIIAHRL 540
Cdd:TIGR02868 480 LALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
344-557 |
1.24e-56 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 190.37 E-value: 1.24e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 344 IRFDNVSYRY-EEGDGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLTPEQLNSLIS 422
Cdd:cd03248 12 VKFQNVTFAYpTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKVS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 423 VVFQDVWLFDDTLLANIRIARPQATRQEVEEAARAAQCLEFISRLPQGWLTPMGEMGGQLSGGERQRISIARALLKNAPV 502
Cdd:cd03248 92 LVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQV 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1805558896 503 VILDEPTAALDIESELAVQKAIDNLVHNRTVIIIAHRLSTIAGAGNILVIEEGQV 557
Cdd:cd03248 172 LILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
17-576 |
1.27e-56 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 202.87 E-value: 1.27e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 17 RQLISSVGSQARMLRRSMLALLLAAFMQGI------AFACLYpiIDALLRGDAPQLLN---WAMAFSvaAIVTLVLRWYG 87
Cdd:TIGR03796 139 PSLLRALWRRLRGSRGALLYLLLAGLLLVLpglvipAFSQIF--VDEILVQGRQDWLRpllLGMGLT--ALLQGVLTWLQ 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 88 LGFEYRGHLAQAThELRLRLGEQLRRVPLEKLQRGRAGEMNalllGSVDENLNYVIAIANIL---LLTIVTPLTASLATL 164
Cdd:TIGR03796 215 LYYLRRLEIKLAV-GMSARFLWHILRLPVRFFAQRHAGDIA----SRVQLNDQVAEFLSGQLattALDAVMLVFYALLML 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 165 WIDWRLGLVMLLIFPLLVPFYYW----RRPAMRRQMQTLGeahqRLSGDIVEFAQGMMVLRTCGSDAD--------KSRA 232
Cdd:TIGR03796 290 LYDPVLTLIGIAFAAINVLALQLvsrrRVDANRRLQQDAG----KLTGVAISGLQSIETLKASGLESDffsrwagyQAKL 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 233 LlahfNALENLQTRTHRQGAGATML--IASVVELGLqvvvlsGIVWVVTGTLNLAFLIAAVAMIMRFAEPMAMFISYTSV 310
Cdd:TIGR03796 366 L----NAQQELGVLTQILGVLPTLLtsLNSALILVV------GGLRVMEGQLTIGMLVAFQSLMSSFLEPVNNLVGFGGT 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 311 VELIASALQRIERFMAIAPLPVAE-------QSEMPERYD--IRFDNVSYRYEEGDGHALNHVSLTFPAASMSALVGASG 381
Cdd:TIGR03796 436 LQELEGDLNRLDDVLRNPVDPLLEepegsaaTSEPPRRLSgyVELRNITFGYSPLEPPLIENFSLTLQPGQRVALVGGSG 515
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 382 AGKTTVTKLLMRYADPQQGQISIGGVDIRRLTPEQLNSLISVVFQDVWLFDDTLLANIRIARPQATRQEVEEAARAAQCL 461
Cdd:TIGR03796 516 SGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVLANSVAMVDQDIFLFEGTVRDNLTLWDPTIPDADLVRACKDAAIH 595
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 462 EFISRLPQGWLTPMGEMGGQLSGGERQRISIARALLKNAPVVILDEPTAALDIESELAVqkaIDNLvHNR--TVIIIAHR 539
Cdd:TIGR03796 596 DVITSRPGGYDAELAEGGANLSGGQRQRLEIARALVRNPSILILDEATSALDPETEKII---DDNL-RRRgcTCIIVAHR 671
|
570 580 590
....*....|....*....|....*....|....*..
gi 1805558896 540 LSTIAGAGNILVIEEGQVVEQGTHAQLLSHHGRYQAL 576
Cdd:TIGR03796 672 LSTIRDCDEIIVLERGKVVQRGTHEELWAVGGAYARL 708
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
161-582 |
3.32e-56 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 199.56 E-value: 3.32e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 161 LATLWIDWRLGLVMLLIFP--LLVPFYYWR--RPAMRRQMQTLGEahqrLSGDIVEFAQGMMVLRTCGSDAdksrallaH 236
Cdd:PRK10790 158 VAMFSLDWRMALVAIMIFPavLVVMVIYQRysTPIVRRVRAYLAD----INDGFNEVINGMSVIQQFRQQA--------R 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 237 FNALENLQTRTHRQGAGATM------------LIASVVELGLqvVVLSGIVWVvtGTLNLAFLIAAVAMIMRFAEPMAMF 304
Cdd:PRK10790 226 FGERMGEASRSHYMARMQTLrldgfllrpllsLFSALILCGL--LMLFGFSAS--GTIEVGVLYAFISYLGRLNEPLIEL 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 305 ISYTSVVELIASALQRIERFMAIAPLPVAEQSEMPERYDIRFDNVSYRYEEgDGHALNHVSLTFPAASMSALVGASGAGK 384
Cdd:PRK10790 302 TTQQSMLQQAVVAGERVFELMDGPRQQYGNDDRPLQSGRIDIDNVSFAYRD-DNLVLQNINLSVPSRGFVALVGHTGSGK 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 385 TTVTKLLMRYADPQQGQISIGGVDIRRLTPEQLNSLISVVFQDVWLFDDTLLANIRIARPqATRQEVEEAARAAQCLEFI 464
Cdd:PRK10790 381 STLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGRD-ISEEQVWQALETVQLAELA 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 465 SRLPQGWLTPMGEMGGQLSGGERQRISIARALLKNAPVVILDEPTAALDIESELAVQKAIDNLVHNRTVIIIAHRLSTIA 544
Cdd:PRK10790 460 RSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIV 539
|
410 420 430
....*....|....*....|....*....|....*...
gi 1805558896 545 GAGNILVIEEGQVVEQGTHAQLLSHHGRYQALWQAQMA 582
Cdd:PRK10790 540 EADTILVLHRGQAVEQGTHQQLLAAQGRYWQMYQLQLA 577
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
54-576 |
5.98e-56 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 201.10 E-value: 5.98e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 54 IIDALL-RGDAPQLLN--WAMA-FSVAAIVTLVLRwyGLGFEYRghLAQATHELRLRLGEQLRRVPLEKLQRGRAGEMNA 129
Cdd:TIGR00958 187 VIDTLGgDKGPPALASaiFFMClLSIASSVSAGLR--GGSFNYT--MARINLRIREDLFRSLLRQDLGFFDENKTGELTS 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 130 LLLGSVDENLNYVIAIANILLLTIVTPLTASLATLWIDWRLGLVMLLIFPLLV----PFYYWRRPAMRRQMQTLGEahqr 205
Cdd:TIGR00958 263 RLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWLSPRLTMVTLINLPLVFlaekVFGKRYQLLSEELQEAVAK---- 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 206 lSGDIVEFAQGMMvlRTCGSDADKSRALLAHFNALEN-LQTRTHRQGAGATML-IASVVELGLQVVVLS-GIVWVVTGTL 282
Cdd:TIGR00958 339 -ANQVAEEALSGM--RTVRSFAAEEGEASRFKEALEEtLQLNKRKALAYAGYLwTTSVLGMLIQVLVLYyGGQLVLTGKV 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 283 NLAFLIAAVAMIMRFAEPMAMFIS-YTSVVELIASAlQRIERFMAIAPLPVAEQSEMPERYD--IRFDNVSYRY-EEGDG 358
Cdd:TIGR00958 416 SSGNLVSFLLYQEQLGEAVRVLSYvYSGMMQAVGAS-EKVFEYLDRKPNIPLTGTLAPLNLEglIEFQDVSFSYpNRPDV 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 359 HALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLTPEQLNSLISVVFQDVWLFDDTLLAN 438
Cdd:TIGR00958 495 PVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVREN 574
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 439 IRIARPQATRQEVEEAARAAQCLEFISRLPQGWLTPMGEMGGQLSGGERQRISIARALLKNAPVVILDEPTAALDIESEL 518
Cdd:TIGR00958 575 IAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQ 654
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1805558896 519 AVQKaiDNLVHNRTVIIIAHRLSTIAGAGNILVIEEGQVVEQGTHAQLLSHHGRYQAL 576
Cdd:TIGR00958 655 LLQE--SRSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYKHL 710
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
252-572 |
8.95e-56 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 197.66 E-value: 8.95e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 252 AGATMLIASVVELGLQVVVLS-GIVWVVTGTLNLAFLIAAVAMIMRFAEPMAMFISYTSVVELIASALQRIERFMAIAPL 330
Cdd:COG4618 238 AGGFSALSKFLRLLLQSAVLGlGAYLVIQGEITPGAMIAASILMGRALAPIEQAIGGWKQFVSARQAYRRLNELLAAVPA 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 331 PvAEQSEMPE-RYDIRFDNVSYRYEEGDGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDI 409
Cdd:COG4618 318 E-PERMPLPRpKGRLSVENLTVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADL 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 410 RRLTPEQLNSLISVVFQDVWLFDDTLLANIriAR-PQATRQEVEEAARAAQCLEFISRLPQGWLTPMGEMGGQLSGGERQ 488
Cdd:COG4618 397 SQWDREELGRHIGYLPQDVELFDGTIAENI--ARfGDADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQ 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 489 RISIARALLKNAPVVILDEPTAALDIESELAVQKAIDNL-VHNRTVIIIAHRLSTIAGAGNILVIEEGQVVEQGTHAQLL 567
Cdd:COG4618 475 RIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALkARGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVL 554
|
....*
gi 1805558896 568 SHHGR 572
Cdd:COG4618 555 ARLAR 559
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
357-584 |
7.64e-51 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 184.66 E-value: 7.64e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 357 DGHAL-NHVSLTFPAASMSALVGASGAGKTTVTKLLMRYAdPQQGQISIGGVDIRRLTPEQLNSLISVVFQDVWLFDDTL 435
Cdd:PRK11174 361 DGKTLaGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTL 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 436 LANIRIARPQATRQEVEEAARAAQCLEFISRLPQGWLTPMGEMGGQLSGGERQRISIARALLKNAPVVILDEPTAALDIE 515
Cdd:PRK11174 440 RDNVLLGNPDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAH 519
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1805558896 516 SELAVQKAIDNLVHNRTVIIIAHRLSTIAGAGNILVIEEGQVVEQGTHAQLLSHHGRYQALWQAQMAAR 584
Cdd:PRK11174 520 SEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATLLAHRQEEI 588
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
344-561 |
7.31e-47 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 162.48 E-value: 7.31e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 344 IRFDNVSYRYEEGDGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLTpEQLNSLISV 423
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 424 VFQDVWLFDDTLLANIriarpqatrqeveeaaraaqclefisrlpqgwltpmgemGGQLSGGERQRISIARALLKNAPVV 503
Cdd:cd03247 80 LNQRPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQDAPIV 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1805558896 504 ILDEPTAALDIESELAVQKAIDNLVHNRTVIIIAHRLSTIAGAGNILVIEEGQVVEQG 561
Cdd:cd03247 121 LLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
252-569 |
2.19e-46 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 171.38 E-value: 2.19e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 252 AGATMLIASVVELGLQVVVLS-GIVWVVTGTLNLAFLIAAVAMIMRFAEPMAMFISYTSVVELIASALQRIERFMAIAPL 330
Cdd:TIGR01842 224 AGMLSNLSKYFRIVLQSLVLGlGAYLAIDGEITPGMMIAGSILVGRALAPIDGAIGGWKQFSGARQAYKRLNELLANYPS 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 331 PvAEQSEMPE-RYDIRFDNVSYRYEEGDGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDI 409
Cdd:TIGR01842 304 R-DPAMPLPEpEGHLSVENVTIVPPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADL 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 410 RRLTPEQLNSLISVVFQDVWLFDDTLLANIRIARPQATRQEVEEAARAAQCLEFISRLPQGWLTPMGEMGGQLSGGERQR 489
Cdd:TIGR01842 383 KQWDRETFGKHIGYLPQDVELFPGTVAENIARFGENADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQR 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 490 ISIARALLKNAPVVILDEPTAALDIESELAVQKAIDNL-VHNRTVIIIAHRLSTIAGAGNILVIEEGQVVEQGTHAQLLS 568
Cdd:TIGR01842 463 IALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALkARGITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLA 542
|
.
gi 1805558896 569 H 569
Cdd:TIGR01842 543 K 543
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
344-570 |
2.07e-45 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 160.19 E-value: 2.07e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 344 IRFDNVSYRYEEGDgHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLTPEQLNSLISV 423
Cdd:COG1122 1 IELENLSFSYPGGT-PALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 424 VFQDVW--LFDDTL-------LANIRIARPQAtRQEVEEAARAAQCLEFISRLPQgwltpmgemggQLSGGERQRISIAR 494
Cdd:COG1122 80 VFQNPDdqLFAPTVeedvafgPENLGLPREEI-RERVEEALELVGLEHLADRPPH-----------ELSGGQKQRVAIAG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1805558896 495 ALLKNAPVVILDEPTAALDIESELAVQKAIDNLVH-NRTVIIIAHRLSTIAG-AGNILVIEEGQVVEQGTHAQLLSHH 570
Cdd:COG1122 148 VLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKeGKTVIIVTHDLDLVAElADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
344-565 |
3.48e-43 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 154.05 E-value: 3.48e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 344 IRFDNVSYRYEeGDGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLTPEQLNSL--- 420
Cdd:COG2884 2 IRFENVSKRYP-GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYLrrr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 421 ISVVFQDVWLFDD-TLLANIRIA------RPQATRQEVEEAARAAQCLEFISRLPQgwltpmgemggQLSGGERQRISIA 493
Cdd:COG2884 81 IGVVFQDFRLLPDrTVYENVALPlrvtgkSRKEIRRRVREVLDLVGLSDKAKALPH-----------ELSGGEQQRVAIA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1805558896 494 RALLKNAPVVILDEPTAALDIESELAVQKAIDNLVHNRTVIIIA-HRLSTIAGAGN-ILVIEEGQVVEQGTHAQ 565
Cdd:COG2884 150 RALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIAtHDLELVDRMPKrVLELEDGRLVRDEARGV 223
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
344-557 |
4.21e-42 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 149.29 E-value: 4.21e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 344 IRFDNVSYRYEEGDGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLTPEQLNSLISV 423
Cdd:cd03246 1 LEVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 424 VFQDVWLFDDTLLANIriarpqatrqeveeaaraaqclefisrlpqgwltpmgemggqLSGGERQRISIARALLKNAPVV 503
Cdd:cd03246 81 LPQDDELFSGSIAENI------------------------------------------LSGGQRQRLGLARALYGNPRIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1805558896 504 ILDEPTAALDIESELAVQKAIDNL-VHNRTVIIIAHRLSTIAGAGNILVIEEGQV 557
Cdd:cd03246 119 VLDEPNSHLDVEGERALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
344-561 |
1.70e-41 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 149.58 E-value: 1.70e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 344 IRFDNVSYRYEEGDGH--ALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLTPEQLNSL- 420
Cdd:cd03257 2 LEVKNLSVSFPTGGGSvkALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIRr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 421 --ISVVFQD-------VWLFDDTLLANIRIARPQATRQEVEEAARAAQCL-----EFISRLPQgwltpmgemggQLSGGE 486
Cdd:cd03257 82 keIQMVFQDpmsslnpRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGvglpeEVLNRYPH-----------ELSGGQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 487 RQRISIARALLKNAPVVILDEPTAALDIeselAVQKAIDNLV------HNRTVIIIAHRLSTIAG-AGNILVIEEGQVVE 559
Cdd:cd03257 151 RQRVAIARALALNPKLLIADEPTSALDV----SVQAQILDLLkklqeeLGLTLLFITHDLGVVAKiADRVAVMYAGKIVE 226
|
..
gi 1805558896 560 QG 561
Cdd:cd03257 227 EG 228
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
344-570 |
3.10e-41 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 149.06 E-value: 3.10e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 344 IRFDNVSYRYeeGDGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLtPEQLNSLISV 423
Cdd:COG1131 1 IEVRGLTKRY--GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARD-PAEVRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 424 VFQDVWLFDD-TLLANIR-IAR-----PQATRQEVEEAARAAQCLEFISRLPqgwltpmgemgGQLSGGERQRISIARAL 496
Cdd:COG1131 78 VPQEPALYPDlTVRENLRfFARlyglpRKEARERIDELLELFGLTDAADRKV-----------GTLSGGMKQRLGLALAL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1805558896 497 LKNAPVVILDEPTAALDIESELAVQKAIDNLV-HNRTVIIIAHRLSTI-AGAGNILVIEEGQVVEQGTHAQLLSHH 570
Cdd:COG1131 147 LHDPELLILDEPTSGLDPEARRELWELLRELAaEGKTVLLSTHYLEEAeRLCDRVAIIDKGRIVADGTPDELKARL 222
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
345-556 |
5.78e-41 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 147.61 E-value: 5.78e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 345 RFDNVSYRYEEGDGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLTPEQLNSLISVV 424
Cdd:cd03225 1 ELKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 425 FQ--DVWLFDDTL-------LANIRIARPQAtRQEVEEAARAAQCLEFISRLPQgwltpmgemggQLSGGERQRISIARA 495
Cdd:cd03225 81 FQnpDDQFFGPTVeeevafgLENLGLPEEEI-EERVEEALELVGLEGLRDRSPF-----------TLSGGQKQRVAIAGV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1805558896 496 LLKNAPVVILDEPTAALDIESELAVQKAIDNLVH-NRTVIIIAHRLSTIAGAGN-ILVIEEGQ 556
Cdd:cd03225 149 LAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAeGKTIIIVTHDLDLLLELADrVIVLEDGK 211
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
344-569 |
9.35e-41 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 155.06 E-value: 9.35e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 344 IRFDNVSYRYEEGDG---HALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLTPEQLNSL 420
Cdd:COG1123 261 LEVRNLSKRYPVRGKggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 421 ---ISVVFQD----------VWlfdDTL---LANIRIARPQATRQEVEEAARAAQ-CLEFISRLPqgwltpmgemgGQLS 483
Cdd:COG1123 341 rrrVQMVFQDpysslnprmtVG---DIIaepLRLHGLLSRAERRERVAELLERVGlPPDLADRYP-----------HELS 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 484 GGERQRISIARALLKNAPVVILDEPTAALDieseLAVQKAIDNLV------HNRTVIIIAHRLSTIAG-AGNILVIEEGQ 556
Cdd:COG1123 407 GGQRQRVAIARALALEPKLLILDEPTSALD----VSVQAQILNLLrdlqreLGLTYLFISHDLAVVRYiADRVAVMYDGR 482
|
250
....*....|...
gi 1805558896 557 VVEQGTHAQLLSH 569
Cdd:COG1123 483 IVEDGPTEEVFAN 495
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
344-560 |
2.75e-40 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 146.34 E-value: 2.75e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 344 IRFDNVSYRYEEGDG--HALNHVSLTFPAASMSALVGASGAGKTTVTKL---LMRyadPQQGQISIGGVDIRRLTPEQL- 417
Cdd:COG1136 5 LELRNLTKSYGTGEGevTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNIlggLDR---PTSGEVLIDGQDISSLSERELa 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 418 ---NSLISVVFQDVWLFDD-TLLANIRIA------RPQATRQEVEEAARAAQCLEFISRLPqgwltpmgemgGQLSGGER 487
Cdd:COG1136 82 rlrRRHIGFVFQFFNLLPElTALENVALPlllagvSRKERRERARELLERVGLGDRLDHRP-----------SQLSGGQQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1805558896 488 QRISIARALLKNAPVVILDEPTAALDIESELAVQKAIDNLV--HNRTVIIIAHRLSTIAGAGNILVIEEGQVVEQ 560
Cdd:COG1136 151 QRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNreLGTTIVMVTHDPELAARADRVIRLRDGRIVSD 225
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
339-562 |
8.48e-40 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 144.48 E-value: 8.48e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 339 PERYDIRFDNVSYRYEEGDGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLTPEQLN 418
Cdd:cd03369 2 PEHGEIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 419 SLISVVFQDVWLFDDTLLANIRIARPQaTRQEVEEAARAAqclefisrlpqgwltpmgEMGGQLSGGERQRISIARALLK 498
Cdd:cd03369 82 SSLTIIPQDPTLFSGTIRSNLDPFDEY-SDEEIYGALRVS------------------EGGLNLSQGQRQLLCLARALLK 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1805558896 499 NAPVVILDEPTAALDIESELAVQKAIDNLVHNRTVIIIAHRLSTIAGAGNILVIEEGQVVEQGT 562
Cdd:cd03369 143 RPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
344-557 |
1.02e-39 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 144.55 E-value: 1.02e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 344 IRFDNVSYRYEEGDG--HALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLTPEQLNSL- 420
Cdd:cd03255 1 IELKNLSKTYGGGGEkvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 421 ---ISVVFQDVWLFDD-TLLANIRIARPQATRQEVEEAARAAQCLE------FISRLPqgwltpmgemgGQLSGGERQRI 490
Cdd:cd03255 81 rrhIGFVFQSFNLLPDlTALENVELPLLLAGVPKKERRERAEELLErvglgdRLNHYP-----------SELSGGQQQRV 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1805558896 491 SIARALLKNAPVVILDEPTAALDIESELAVQKAIDNLVHNR--TVIIIAHRLSTIAGAGNILVIEEGQV 557
Cdd:cd03255 150 AIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAgtTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
344-572 |
1.17e-39 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 145.00 E-value: 1.17e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 344 IRFDNVSYRYeeGDGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLtPEQLNSLISV 423
Cdd:COG4555 2 IEVENLSKKY--GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKE-PREARRQIGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 424 VFQDVWLFDD-TLLANIRI---ARPQATRQEVEEAARAAQCLEFISRLPQGWltpmgemgGQLSGGERQRISIARALLKN 499
Cdd:COG4555 79 LPDERGLYDRlTVRENIRYfaeLYGLFDEELKKRIEELIELLGLEEFLDRRV--------GELSTGMKKKVALARALVHD 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1805558896 500 APVVILDEPTAALDIESELAVQKAIDNLV-HNRTVIIIAHRLSTIAG-AGNILVIEEGQVVEQGTHAQLLSHHGR 572
Cdd:COG4555 151 PKVLLLDEPTNGLDVMARRLLREILRALKkEGKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIGE 225
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
344-594 |
1.44e-38 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 148.90 E-value: 1.44e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 344 IRFDNVSYRYEEGDGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQ---QGQISIGGVDIRRLTPEQLNSL 420
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 421 ISVVFQDVWLFDDTL---------LANIRIARPQAtRQEVEEAARAAQCLEFISRLPQgwltpmgemggQLSGGERQRIS 491
Cdd:COG1123 85 IGMVFQDPMTQLNPVtvgdqiaeaLENLGLSRAEA-RARVLELLEAVGLERRLDRYPH-----------QLSGGQRQRVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 492 IARALLKNAPVVILDEPTAALDIESELAVQKAIDNLV--HNRTVIIIAHRLSTIAG-AGNILVIEEGQVVEQGTHAQLLS 568
Cdd:COG1123 153 IAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQreRGTTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPEEILA 232
|
250 260
....*....|....*....|....*.
gi 1805558896 569 HHGRYQALWQAQMAARVWRDDGVSAS 594
Cdd:COG1123 233 APQALAAVPRLGAARGRAAPAAAAAE 258
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
344-569 |
3.40e-38 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 140.71 E-value: 3.40e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 344 IRFDNVSYRYeeGDGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLTPEQLNSL--- 420
Cdd:cd03261 1 IELRGLTKSF--GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLrrr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 421 ISVVFQDVWLFDD-TLLANIriARP-----QATRQEVEEaaRAAQCLEFISRLPQGWLTPmgemgGQLSGGERQRISIAR 494
Cdd:cd03261 79 MGMLFQSGALFDSlTVFENV--AFPlrehtRLSEEEIRE--IVLEKLEAVGLRGAEDLYP-----AELSGGMKKRVALAR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 495 ALLKNAPVVILDEPTAALD-IESElavqkAIDNLVH------NRTVIIIAHRLSTIAGAG-NILVIEEGQVVEQGTHAQL 566
Cdd:cd03261 150 ALALDPELLLYDEPTAGLDpIASG-----VIDDLIRslkkelGLTSIMVTHDLDTAFAIAdRIAVLYDGKIVAEGTPEEL 224
|
...
gi 1805558896 567 LSH 569
Cdd:cd03261 225 RAS 227
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
344-570 |
1.26e-37 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 139.55 E-value: 1.26e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 344 IRFDNVSYRYEEGDG--HALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLTPEQLNSLI 421
Cdd:COG1124 2 LEVRNLSVSYGQGGRrvPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 422 SVVFQD-------VWLFDDTLLANIRIARPQATRQEVEEAARAAQ-CLEFISRLPQgwltpmgemggQLSGGERQRISIA 493
Cdd:COG1124 82 QMVFQDpyaslhpRHTVDRILAEPLRIHGLPDREERIAELLEQVGlPPSFLDRYPH-----------QLSGGQRQRVAIA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 494 RALLKNAPVVILDEPTAALDieseLAVQKAIDNLV------HNRTVIIIAHRLSTIAG-AGNILVIEEGQVVEQGTHAQL 566
Cdd:COG1124 151 RALILEPELLLLDEPTSALD----VSVQAEILNLLkdlreeRGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVADL 226
|
....
gi 1805558896 567 LSHH 570
Cdd:COG1124 227 LAGP 230
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
361-510 |
2.84e-37 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 135.47 E-value: 2.84e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 361 LNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLTPEQLNSLISVVFQDVWLFDD-TLLANI 439
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1805558896 440 RIARPQATRQEVEEAARAAqclEFISRLPQGWL--TPMGEMGGQLSGGERQRISIARALLKNAPVVILDEPTA 510
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAE---EALEKLGLGDLadRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
345-556 |
2.99e-37 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 135.45 E-value: 2.99e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 345 RFDNVSYRYeeGDGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLTPEQLNSLISVV 424
Cdd:cd00267 1 EIENLSFRY--GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 425 FQdvwlfddtllaniriarpqatrqeveeaaraaqclefisrlpqgwltpmgemggqLSGGERQRISIARALLKNAPVVI 504
Cdd:cd00267 79 PQ-------------------------------------------------------LSGGQRQRVALARALLLNPDLLL 103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1805558896 505 LDEPTAALDIESELAVQKAIDNLV-HNRTVIIIAHRLSTIAGAGN-ILVIEEGQ 556
Cdd:cd00267 104 LDEPTSGLDPASRERLLELLRELAeEGRTVIIVTHDPELAELAADrVIVLKDGK 157
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
344-567 |
7.49e-37 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 137.42 E-value: 7.49e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 344 IRFDNVSYRYeeGDGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLTPEQLNSL--- 420
Cdd:COG1127 6 IEVRNLTKSF--GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYELrrr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 421 ISVVFQDVWLFDD-TLLANIR---IARPQATRQEVEEaaRAAQCLE------FISRLPqgwltpmgemgGQLSGGERQRI 490
Cdd:COG1127 84 IGMLFQGGALFDSlTVFENVAfplREHTDLSEAEIRE--LVLEKLElvglpgAADKMP-----------SELSGGMRKRV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 491 SIARALLKNAPVVILDEPTAALDIESELAVQKAIDNLVHNR--TVIIIAHRLSTI-AGAGNILVIEEGQVVEQGTHAQLL 567
Cdd:COG1127 151 ALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELglTSVVVTHDLDSAfAIADRVAVLADGKIIAEGTPEELL 230
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
344-557 |
1.19e-36 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 135.71 E-value: 1.19e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 344 IRFDNVSYRYEEGDGhaLNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLTPEQLNSLISV 423
Cdd:COG4619 1 LELEGLSFRVGGKPI--LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 424 VFQDVWLFDDTLLANIRiaRPQATRQEVEEAARAAQCLEFISRLPQGWLTPMGEmggqLSGGERQRISIARALLKNAPVV 503
Cdd:COG4619 79 VPQEPALWGGTVRDNLP--FPFQLRERKFDRERALELLERLGLPPDILDKPVER----LSGGERQRLALIRALLLQPDVL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1805558896 504 ILDEPTAALDIESELAVQKAIDNLV--HNRTVIIIAH------RLstiagAGNILVIEEGQV 557
Cdd:COG4619 153 LLDEPTSALDPENTRRVEELLREYLaeEGRAVLWVSHdpeqieRV-----ADRVLTLEAGRL 209
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
344-568 |
1.91e-36 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 136.71 E-value: 1.91e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 344 IRFDNVSYRYeeGDGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLTPEQLNSLISV 423
Cdd:COG1120 2 LEAENLSVGY--GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 424 VFQDVwlfddTLLANI---------------RIARPQAT-RQEVEEAARAAQCLEFISRlpqgwltPMGEmggqLSGGER 487
Cdd:COG1120 80 VPQEP-----PAPFGLtvrelvalgryphlgLFGRPSAEdREAVEEALERTGLEHLADR-------PVDE----LSGGER 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 488 QRISIARALLKNAPVVILDEPTAALDIESELAVQKAIDNLVH--NRTVIIIAHRLSTIAG-AGNILVIEEGQVVEQGTHA 564
Cdd:COG1120 144 QRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARerGRTVVMVLHDLNLAARyADRLVLLKDGRIVAQGPPE 223
|
....
gi 1805558896 565 QLLS 568
Cdd:COG1120 224 EVLT 227
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
98-576 |
3.17e-36 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 145.47 E-value: 3.17e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 98 QATHELRLRLGEQLRRVPLEKLQRGRAGEMNALL---LGSVDENLNYVI---------AIANILLLTIVTPLTAslatlw 165
Cdd:TIGR00957 1035 QASRVLHQDLLHNKLRSPMSFFERTPSGNLVNRFskeLDTVDSMIPPVIkmfmgslfnVIGALIVILLATPIAA------ 1108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 166 idwrlglvmLLIFPLLVPFYYWRR--PAMRRQMQTLgEAHQR--LSGDIVEFAQGMMVLRTcgsdADKSRALLAHFNALE 241
Cdd:TIGR00957 1109 ---------VIIPPLGLLYFFVQRfyVASSRQLKRL-ESVSRspVYSHFNETLLGVSVIRA----FEEQERFIHQSDLKV 1174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 242 NLQTRTHRQGAGATMLIASVVELGLQVVVLSGIVWVVTG--TLNLAFLIAAVAMIMRFAEPMAMFISYTSVVELIASALQ 319
Cdd:TIGR00957 1175 DENQKAYYPSIVANRWLAVRLECVGNCIVLFAALFAVISrhSLSAGLVGLSVSYSLQVTFYLNWLVRMSSEMETNIVAVE 1254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 320 RIERFMAI---APLPVAEQ---SEMPERYDIRFDNVSYRYEEGDGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMR 393
Cdd:TIGR00957 1255 RLKEYSETekeAPWQIQETappSGWPPRGRVEFRNYCLRYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFR 1334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 394 YADPQQGQISIGGVDIRRLTPEQLNSLISVVFQDVWLFDDTLLANIRiARPQATRQEVEEAARAAQCLEFISRLPQGWLT 473
Cdd:TIGR00957 1335 INESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLD-PFSQYSDEEVWWALELAHLKTFVSALPDKLDH 1413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 474 PMGEMGGQLSGGERQRISIARALLKNAPVVILDEPTAALDIESELAVQKAIDNLVHNRTVIIIAHRLSTIAGAGNILVIE 553
Cdd:TIGR00957 1414 ECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLD 1493
|
490 500
....*....|....*....|...
gi 1805558896 554 EGQVVEQGTHAQLLSHHGRYQAL 576
Cdd:TIGR00957 1494 KGEVAEFGAPSNLLQQRGIFYSM 1516
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
31-507 |
7.00e-36 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 141.47 E-value: 7.00e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 31 RRSMLALLLAAFMQGIAFACLYPIIDALLRGDAPQLLNWAMAFSVAAIVTLVLRWY-GLGFEYRGHlaQATHELRLRLGE 109
Cdd:COG4615 12 RWLLLLALLLGLLSGLANAGLIALINQALNATGAALARLLLLFAGLLVLLLLSRLAsQLLLTRLGQ--HAVARLRLRLSR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 110 QLRRVPLEKLQRGRAGEMNALLLGSVDenlnyVIAIANILLLTIVTPLTASLATL----WIDWRLGLVMLLIFPLLVPFY 185
Cdd:COG4615 90 RILAAPLERLERIGAARLLAALTEDVR-----TISQAFVRLPELLQSVALVLGCLaylaWLSPPLFLLTLVLLGLGVAGY 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 186 YWRRPAMRRQMQTLGEAHQRLSGDIVEFAQGMMVLRTcgsDADKSRALL-----AHFNALENLQTRTHRQGAGATMLIAS 260
Cdd:COG4615 165 RLLVRRARRHLRRAREAEDRLFKHFRALLEGFKELKL---NRRRRRAFFdedlqPTAERYRDLRIRADTIFALANNWGNL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 261 VVeLGLQVVVLSGIVWVVTGTLNLAFLIAAVAMIMRfaEPMAMFISYTSVVELIASALQRIERFM-----AIAPLPVAEQ 335
Cdd:COG4615 242 LF-FALIGLILFLLPALGWADPAVLSGFVLVLLFLR--GPLSQLVGALPTLSRANVALRKIEELElalaaAEPAAADAAA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 336 SEMPERYD-IRFDNVSYRY--EEGDGH-ALNHVSLTFPAASMSALVGASGAGKTTVTKLLMR-YAdPQQGQISIGGVDIR 410
Cdd:COG4615 319 PPAPADFQtLELRGVTYRYpgEDGDEGfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGlYR-PESGEILLDGQPVT 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 411 RLTPEQLNSLISVVFQDVWLFDDTLlaniriarpqaTRQEVEEAARAAQCLEfisRLpqgwltpmgEMGG---------- 480
Cdd:COG4615 398 ADNREAYRQLFSAVFSDFHLFDRLL-----------GLDGEADPARARELLE---RL---------ELDHkvsvedgrfs 454
|
490 500
....*....|....*....|....*....
gi 1805558896 481 --QLSGGERQRISIARALLKNAPVVILDE 507
Cdd:COG4615 455 ttDLSQGQRKRLALLVALLEDRPILVFDE 483
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
344-570 |
7.38e-36 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 134.50 E-value: 7.38e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 344 IRFDNVSYRYeegdGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLTPEQlnSLISV 423
Cdd:COG3840 2 LRLDDLTYRY----GDFPLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE--RPVSM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 424 VFQDVWLFDD-TLLANIRIA-RP-----QATRQEVEEAARAAQCLEFISRLPqgwltpmgemgGQLSGGERQRISIARAL 496
Cdd:COG3840 76 LFQENNLFPHlTVAQNIGLGlRPglkltAEQRAQVEQALERVGLAGLLDRLP-----------GQLSGGQRQRVALARCL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 497 LKNAPVVILDEPTAALDIeselAVQKAIDNLV------HNRTVIIIAHRLSTIAG-AGNILVIEEGQVVEQGTHAQLLSH 569
Cdd:COG3840 145 VRKRPILLLDEPFSALDP----ALRQEMLDLVdelcreRGLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALLDG 220
|
.
gi 1805558896 570 H 570
Cdd:COG3840 221 E 221
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
344-561 |
9.32e-36 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 133.41 E-value: 9.32e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 344 IRFDNVSYRYeeGDGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLTPEQLNslISV 423
Cdd:cd03259 1 LELKGLSKTY--GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRN--IGM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 424 VFQDVWLFDD-TLLANIRIA-----RPQATRQE-VEEAARAAQCLEFISRLPqgwltpmgemgGQLSGGERQRISIARAL 496
Cdd:cd03259 77 VFQDYALFPHlTVAENIAFGlklrgVPKAEIRArVRELLELVGLEGLLNRYP-----------HELSGGQQQRVALARAL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1805558896 497 LKNAPVVILDEPTAALDIESELAVQKAIDNLVHNR--TVIIIAHRLS-TIAGAGNILVIEEGQVVEQG 561
Cdd:cd03259 146 AREPSLLLLDEPLSALDAKLREELREELKELQRELgiTTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
344-569 |
1.15e-35 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 133.97 E-value: 1.15e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 344 IRFDNVSYRYeeGDGH-ALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLTPEQLNSLIS 422
Cdd:cd03295 1 IEFENVTKRY--GGGKkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 423 VVFQDVWLFDD-TLLANIRIArPQATRQEVEE-AARAAQCLEFISRLPQGWltpMGEMGGQLSGGERQRISIARALLKNA 500
Cdd:cd03295 79 YVIQQIGLFPHmTVEENIALV-PKLLKWPKEKiRERADELLALVGLDPAEF---ADRYPHELSGGQQQRVGVARALAADP 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1805558896 501 PVVILDEPTAALDIESELAVQKAIDNLVH--NRTVIIIAHRL-STIAGAGNILVIEEGQVVEQGTHAQLLSH 569
Cdd:cd03295 155 PLLLMDEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEILRS 226
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
347-561 |
1.28e-34 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 129.09 E-value: 1.28e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 347 DNVSYRYeeGDGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLTPEQLNSLISVVFQ 426
Cdd:cd03214 3 ENLSVGY--GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 427 dvwlfddtllaniriarpqatrqeveeAARAAQCLEFISRlpqgwltPMGEmggqLSGGERQRISIARALLKNAPVVILD 506
Cdd:cd03214 81 ---------------------------ALELLGLAHLADR-------PFNE----LSGGERQRVLLARALAQEPPILLLD 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1805558896 507 EPTAALDIESELAVQKAIDNLV--HNRTVIIIAHRLSTIAG-AGNILVIEEGQVVEQG 561
Cdd:cd03214 123 EPTSHLDIAHQIELLELLRRLAreRGKTVVMVLHDLNLAARyADRVILLKDGRIVAQG 180
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
344-557 |
2.03e-34 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 128.28 E-value: 2.03e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 344 IRFDNVSYRYeeGDGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRlTPEQLNSLISV 423
Cdd:cd03230 1 IEVRNLSKRY--GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 424 VFQDVWLFDD-TLLANIRiarpqatrqeveeaaraaqclefisrlpqgwltpmgemggqLSGGERQRISIARALLKNAPV 502
Cdd:cd03230 78 LPEEPSLYENlTVRENLK-----------------------------------------LSGGMKQRLALAQALLHDPEL 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1805558896 503 VILDEPTAALDIESELAVQKAIDNLV-HNRTVIIIAHRLSTIAG-AGNILVIEEGQV 557
Cdd:cd03230 117 LILDEPTSGLDPESRREFWELLRELKkEGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
344-566 |
2.05e-34 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 129.99 E-value: 2.05e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 344 IRFDNVSYRYeeGDGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYAD-----PQQGQISIGGVDIR--RLTPEQ 416
Cdd:cd03260 1 IELRDLNVYY--GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYdlDVDVLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 417 LNSLISVVFQDVWLFDDTLLANIRIA-RPQATRQEVEEAARAAQCLEfisrlpQGWLTpmGEM-----GGQLSGGERQRI 490
Cdd:cd03260 79 LRRRVGMVFQKPNPFPGSIYDNVAYGlRLHGIKLKEELDERVEEALR------KAALW--DEVkdrlhALGLSGGQQQRL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1805558896 491 SIARALLKNAPVVILDEPTAALDIESELAVQKAIDNLVHNRTVIIIAHRLSTIAG-AGNILVIEEGQVVEQGTHAQL 566
Cdd:cd03260 151 CLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARvADRTAFLLNGRLVEFGPTEQI 227
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
348-569 |
5.71e-34 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 131.71 E-value: 5.71e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 348 NVSYRYEEGDGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQ---QGQISIGGVDIRRLTPEQLNSL---- 420
Cdd:COG0444 8 KVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPgitSGEILFDGEDLLKLSEKELRKIrgre 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 421 ISVVFQD-------VWLFDDTLLANIRIARPqATRQEVEEaaRAAQCLE---------FISRLPqgwltpmgemgGQLSG 484
Cdd:COG0444 88 IQMIFQDpmtslnpVMTVGDQIAEPLRIHGG-LSKAEARE--RAIELLErvglpdperRLDRYP-----------HELSG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 485 GERQRISIARALLKNAPVVILDEPTAALDIeselAVQKAIDNLV------HNRTVIIIAHRLSTIAG-AGNILVIEEGQV 557
Cdd:COG0444 154 GMRQRVMIARALALEPKLLIADEPTTALDV----TIQAQILNLLkdlqreLGLAILFITHDLGVVAEiADRVAVMYAGRI 229
|
250
....*....|..
gi 1805558896 558 VEQGTHAQLLSH 569
Cdd:COG0444 230 VEEGPVEELFEN 241
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
344-569 |
3.36e-33 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 126.93 E-value: 3.36e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 344 IRFDNVSYRYEEGDG--HALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLTPEQLNSL- 420
Cdd:cd03258 2 IELKNVSKVFGDTGGkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKAr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 421 --ISVVFQDVWLFDD-TLLANI----RIARpqATRQEVEEaaRAAQCLEFI------SRLPqgwltpmgemgGQLSGGER 487
Cdd:cd03258 82 rrIGMIFQHFNLLSSrTVFENValplEIAG--VPKAEIEE--RVLELLELVgledkaDAYP-----------AQLSGGQK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 488 QRISIARALLKNAPVVILDEPTAALDIESelavQKAIDNLVH--NR----TVIIIAHRLSTIAGAGN-ILVIEEGQVVEQ 560
Cdd:cd03258 147 QRVGIARALANNPKVLLCDEATSALDPET----TQSILALLRdiNRelglTIVLITHEMEVVKRICDrVAVMEKGEVVEE 222
|
....*....
gi 1805558896 561 GTHAQLLSH 569
Cdd:cd03258 223 GTVEEVFAN 231
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
344-561 |
4.37e-33 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 125.77 E-value: 4.37e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 344 IRFDNVSYRYeeGDGHALNHVSLTFPAAsMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRlTPEQLNSLISV 423
Cdd:cd03264 1 LQLENLTKRY--GKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIGY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 424 VFQD--------VWLFDDTLLANIRIARPQAtRQEVEEAARAAQCLEFISRLPqgwltpmgemgGQLSGGERQRISIARA 495
Cdd:cd03264 77 LPQEfgvypnftVREFLDYIAWLKGIPSKEV-KARVDEVLELVNLGDRAKKKI-----------GSLSGGMRRRVGIAQA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1805558896 496 LLKNAPVVILDEPTAALDIESELAVQKAIDNLVHNRTVIIIAHRLSTIAG-AGNILVIEEGQVVEQG 561
Cdd:cd03264 145 LVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
338-570 |
5.62e-33 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 126.74 E-value: 5.62e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 338 MPERYDIRFDNVSYRYeeGDGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLTPE-- 415
Cdd:COG1121 1 MMMMPAIELENLTVSY--GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRRig 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 416 ---QLNSL-----ISVvfQDVWLFddTLLANIRIARP--QATRQEVEEAARAAQCLEFISRlpqgwltPMGEmggqLSGG 485
Cdd:COG1121 79 yvpQRAEVdwdfpITV--RDVVLM--GRYGRRGLFRRpsRADREAVDEALERVGLEDLADR-------PIGE----LSGG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 486 ERQRISIARALLKNAPVVILDEPTAALDIESELAVQKAIDNLV-HNRTVIIIAHRLSTIAG-AGNILVIeEGQVVEQGTH 563
Cdd:COG1121 144 QQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRrEGKTILVVTHDLGAVREyFDRVLLL-NRGLVAHGPP 222
|
....*..
gi 1805558896 564 AQLLSHH 570
Cdd:COG1121 223 EEVLTPE 229
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
343-569 |
1.16e-32 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 126.18 E-value: 1.16e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 343 DIRFDNVSYRYEEGDGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLTPEQLNSLIS 422
Cdd:cd03288 19 EIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 423 VVFQDVWLFDDTLLANIRIARpQATRQEVEEAARAAQCLEFISRLPQGWLTPMGEMGGQLSGGERQRISIARALLKNAPV 502
Cdd:cd03288 99 IILQDPILFSGSIRFNLDPEC-KCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSI 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1805558896 503 VILDEPTAALDIESELAVQKAIDNLVHNRTVIIIAHRLSTIAGAGNILVIEEGQVVEQGTHAQLLSH 569
Cdd:cd03288 178 LIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQ 244
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
132-571 |
1.49e-32 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 134.33 E-value: 1.49e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 132 LGSVDEN----LNYVIAIANILLLTIVTPLTASLATLWIdwrlglvmllIFPLLVPFY--YWRRPAMRRQMQTL------ 199
Cdd:PLN03232 1017 IGDIDRNvanlMNMFMNQLWQLLSTFALIGTVSTISLWA----------IMPLLILFYaaYLYYQSTSREVRRLdsvtrs 1086
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 200 ------GEAHQRLSGDIVEFAQGMMVLRTCGSDADKSRALLAHFNALENLQTRTHRQGAGATMLIASVVELGL-----QV 268
Cdd:PLN03232 1087 piyaqfGEALNGLSSIRAYKAYDRMAKINGKSMDNNIRFTLANTSSNRWLTIRLETLGGVMIWLTATFAVLRNgnaenQA 1166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 269 VVLSGIVWVVTGTLNLAFLIAAVAMIMRFAEpmamfisytsvveliaSALQRIERFMAIAPLPVAEQ---------SEMP 339
Cdd:PLN03232 1167 GFASTMGLLLSYTLNITTLLSGVLRQASKAE----------------NSLNSVERVGNYIDLPSEATaiiennrpvSGWP 1230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 340 ERYDIRFDNVSYRYEEGDGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLTPEQLNS 419
Cdd:PLN03232 1231 SRGSIKFEDVHLRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRR 1310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 420 LISVVFQDVWLFDDTLLANIRiarPQATRQEVE--EAARAAQCLEFISRLPQGWLTPMGEMGGQLSGGERQRISIARALL 497
Cdd:PLN03232 1311 VLSIIPQSPVLFSGTVRFNID---PFSEHNDADlwEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALL 1387
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1805558896 498 KNAPVVILDEPTAALDIESELAVQKAIDNLVHNRTVIIIAHRLSTIAGAGNILVIEEGQVVEQGTHAQLLSHHG 571
Cdd:PLN03232 1388 RRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDT 1461
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
366-568 |
2.38e-32 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 133.62 E-value: 2.38e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 366 LTFPAAS--MSALVGASGAGKTTVTKLLMRYAD----------------------------------------------- 396
Cdd:PTZ00265 1187 LTFSCDSkkTTAIVGETGSGKSTVMSLLMRFYDlkndhhivfknehtndmtneqdyqgdeeqnvgmknvnefsltkeggs 1266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 397 -------PQQGQISIGGVDIRRLTPEQLNSLISVVFQDVWLFDDTLLANIRIARPQATRQEVEEAARAAQCLEFISRLPQ 469
Cdd:PTZ00265 1267 gedstvfKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKEDATREDVKRACKFAAIDEFIESLPN 1346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 470 GWLTPMGEMGGQLSGGERQRISIARALLKNAPVVILDEPTAALDIESELAVQKAIDNLVH--NRTVIIIAHRLSTIAGAG 547
Cdd:PTZ00265 1347 KYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDkaDKTIITIAHRIASIKRSD 1426
|
250 260
....*....|....*....|....*.
gi 1805558896 548 NILVIEE----GQVVE-QGTHAQLLS 568
Cdd:PTZ00265 1427 KIVVFNNpdrtGSFVQaHGTHEELLS 1452
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
264-571 |
6.07e-32 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 132.55 E-value: 6.07e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 264 LGLQVVVLSGIVWVVTGTLnlafliaAVAMIMR------FAEPMAMFISY--------TSVVELIASA---LQRIERFMA 326
Cdd:PLN03130 1139 LAIRLETLGGLMIWLTASF-------AVMQNGRaenqaaFASTMGLLLSYalnitsllTAVLRLASLAensLNAVERVGT 1211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 327 IAPLP-----VAEQSEMPERY----DIRFDNVSYRYEEGDGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADP 397
Cdd:PLN03130 1212 YIDLPseaplVIENNRPPPGWpssgSIKFEDVVLRYRPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVEL 1291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 398 QQGQISIGGVDIRRLTPEQLNSLISVVFQDVWLFDDTLLANIRiarPQATRQEVE--EAARAAQCLEFISRLPQGWLTPM 475
Cdd:PLN03130 1292 ERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNLD---PFNEHNDADlwESLERAHLKDVIRRNSLGLDAEV 1368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 476 GEMGGQLSGGERQRISIARALLKNAPVVILDEPTAALDIESELAVQKAIDNLVHNRTVIIIAHRLSTIAGAGNILVIEEG 555
Cdd:PLN03130 1369 SEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAG 1448
|
330
....*....|....*.
gi 1805558896 556 QVVEQGTHAQLLSHHG 571
Cdd:PLN03130 1449 RVVEFDTPENLLSNEG 1464
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
344-562 |
1.01e-31 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 122.73 E-value: 1.01e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 344 IRFDNVSYRYeeGDGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLTPEQLNslISV 423
Cdd:cd03300 1 IELENVSKFY--GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRP--VNT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 424 VFQDVWLFDD-TLLANI----RIAR--PQATRQEVEEAARAAQCLEFISRLPQgwltpmgemggQLSGGERQRISIARAL 496
Cdd:cd03300 77 VFQNYALFPHlTVFENIafglRLKKlpKAEIKERVAEALDLVQLEGYANRKPS-----------QLSGGQQQRVAIARAL 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 497 LKNAPVVILDEPTAALDIESELAVQKAIDNLvHNR---TVIIIAHRLS-TIAGAGNILVIEEGQVVEQGT 562
Cdd:cd03300 146 VNEPKVLLLDEPLGALDLKLRKDMQLELKRL-QKElgiTFVFVTHDQEeALTMSDRIAVMNKGKIQQIGT 214
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
344-567 |
2.02e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 123.18 E-value: 2.02e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 344 IRFDNVSYRYEEGDGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLTPEQLNSLISV 423
Cdd:PRK13632 8 IKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 424 VFQD-------VWLFDDTL--LANIRIArPQATRQEVEEAARAAQCLEFISRLPQgwltpmgemggQLSGGERQRISIAR 494
Cdd:PRK13632 88 IFQNpdnqfigATVEDDIAfgLENKKVP-PKKMKDIIDDLAKKVGMEDYLDKEPQ-----------NLSGGQKQRVAIAS 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1805558896 495 ALLKNAPVVILDEPTAALDIESELAVQKAIDNL--VHNRTVIIIAHRLSTIAGAGNILVIEEGQVVEQGTHAQLL 567
Cdd:PRK13632 156 VLALNPEIIIFDESTSMLDPKGKREIKKIMVDLrkTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEIL 230
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
344-561 |
2.17e-31 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 121.06 E-value: 2.17e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 344 IRFDNVSYRYeegdGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLTPEQlnSLISV 423
Cdd:cd03298 1 VRLDKIRFSY----GEQPMHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPAD--RPVSM 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 424 VFQDVWLFDD-TLLANIRIARP------QATRQEVEEAARAAQCLEFISRLPqgwltpmgemgGQLSGGERQRISIARAL 496
Cdd:cd03298 75 LFQENNLFAHlTVEQNVGLGLSpglkltAEDRQAIEVALARVGLAGLEKRLP-----------GELSGGERQRVALARVL 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1805558896 497 LKNAPVVILDEPTAALDIESELAVQKAIDNLVHNR--TVIIIAHRLSTIAG-AGNILVIEEGQVVEQG 561
Cdd:cd03298 144 VRDKPVLLLDEPFAALDPALRAEMLDLVLDLHAETkmTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
344-556 |
3.27e-31 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 119.60 E-value: 3.27e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 344 IRFDNVSYRYeeGDGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLT--PEQLNSLI 421
Cdd:cd03229 1 LELKNVSKRY--GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEdeLPPLRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 422 SVVFQDVWLFDD-TLLANIRIArpqatrqeveeaaraaqclefisrlpqgwltpmgemggqLSGGERQRISIARALLKNA 500
Cdd:cd03229 79 GMVFQDFALFPHlTVLENIALG---------------------------------------LSGGQQQRVALARALAMDP 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1805558896 501 PVVILDEPTAALDIESELAVQKAIDNLV--HNRTVIIIAHRLSTIAG-AGNILVIEEGQ 556
Cdd:cd03229 120 DVLLLDEPTSALDPITRREVRALLKSLQaqLGITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
344-556 |
3.62e-31 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 120.27 E-value: 3.62e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 344 IRFDNVSYRYEEGDGHA---LNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVdirrltpeqlnsl 420
Cdd:cd03250 1 ISVEDASFTWDSGEQETsftLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 421 ISVVFQDVWLFDDTLLANIRIARPqATRQEVEEAARAAQCLEFISRLPQGWLTPMGEMGGQLSGGERQRISIARALLKNA 500
Cdd:cd03250 68 IAYVSQEPWIQNGTIRENILFGKP-FDEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDA 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1805558896 501 PVVILDEPTAALDIESELAV-QKAI-DNLVHNRTVIIIAHRLSTIAGAGNILVIEEGQ 556
Cdd:cd03250 147 DIYLLDDPLSAVDAHVGRHIfENCIlGLLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
331-552 |
9.80e-31 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 128.61 E-value: 9.80e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 331 PVAEQSE----MPERYDIRFDNVSYRYE-EGDGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIG 405
Cdd:PTZ00265 366 PLVENNDdgkkLKDIKKIQFKNVRFHYDtRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIN 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 406 GV-DIRRLTPEQLNSLISVVFQDVWLFDDTLLANIR-----IARPQATRQEVEEAARAAQ------------CL------ 461
Cdd:PTZ00265 446 DShNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKyslysLKDLEALSNYYNEDGNDSQenknkrnscrakCAgdlndm 525
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 462 ----------------------------------EFISRLPQGWLTPMGEMGGQLSGGERQRISIARALLKNAPVVILDE 507
Cdd:PTZ00265 526 snttdsneliemrknyqtikdsevvdvskkvlihDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDE 605
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1805558896 508 PTAALDIESELAVQKAIDNLV--HNRTVIIIAHRLSTIAGAGNILVI 552
Cdd:PTZ00265 606 ATSSLDNKSEYLVQKTINNLKgnENRITIIIAHRLSTIRYANTIFVL 652
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
344-538 |
1.92e-30 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 119.81 E-value: 1.92e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 344 IRFDNVSYRYEEGDG--HALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLTPEqlnslI 421
Cdd:COG1116 8 LELRGVSKRFPTGGGgvTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD-----R 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 422 SVVFQDV----WLfddTLLANIRIARPQATRQEVEEAARAAQCLE------FISRLPqgwltpmgemgGQLSGGERQRIS 491
Cdd:COG1116 83 GVVFQEPallpWL---TVLDNVALGLELRGVPKAERRERARELLElvglagFEDAYP-----------HQLSGGMRQRVA 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1805558896 492 IARALLKNAPVVILDEPTAALDIESELAVQKAIDNLV--HNRTVIIIAH 538
Cdd:COG1116 149 IARALANDPEVLLMDEPFGALDALTRERLQDELLRLWqeTGKTVLFVTH 197
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
345-561 |
3.61e-30 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 117.63 E-value: 3.61e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 345 RFDNVSYRYeeGDGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDirrltPEQLNSLISVV 424
Cdd:cd03235 1 EVEDLTVSY--GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKP-----LEKERKRIGYV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 425 FQ--DV-WLFDDT--------LLANIRIARP--QATRQEVEEAARAAQCLEFISRlpqgwltPMGEmggqLSGGERQRIS 491
Cdd:cd03235 74 PQrrSIdRDFPISvrdvvlmgLYGHKGLFRRlsKADKAKVDEALERVGLSELADR-------QIGE----LSGGQQQRVL 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1805558896 492 IARALLKNAPVVILDEPTAALDIESELAVQKAIDNL-VHNRTVIIIAHRLSTIAGAGNILVIEEGQVVEQG 561
Cdd:cd03235 143 LARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELrREGMTILVVTHDLGLVLEYFDRVLLLNRTVVASG 213
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
359-569 |
6.34e-30 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 117.92 E-value: 6.34e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 359 HALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLTPEQLNSL-ISVVFQDVWLFDD-TLL 436
Cdd:cd03219 14 VALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLgIGRTFQIPRLFPElTVL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 437 ANIRIARPQAT----------RQEVEEAARAAQCLEFIsRLPQGWLTPMGEmggqLSGGERQRISIARALLKNAPVVILD 506
Cdd:cd03219 94 ENVMVAAQARTgsglllararREEREARERAEELLERV-GLADLADRPAGE----LSYGQQRRLEIARALATDPKLLLLD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1805558896 507 EPTAALDIESELAVQKAIDNLV-HNRTVIIIAHRLSTIAG-AGNILVIEEGQVVEQGTHAQLLSH 569
Cdd:cd03219 169 EPAAGLNPEETEELAELIRELReRGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGTPDEVRNN 233
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
344-566 |
1.05e-29 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 117.28 E-value: 1.05e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 344 IRFDNVSYRYEEGDgHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLTPEQLNSL--- 420
Cdd:cd03256 1 IEVENLSKTYPNGK-KALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLrrq 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 421 ISVVFQDVWLFDD-TLLANI---RIA-----RPQATRQEVEEAARAAQCLEFISRLPQGWltpmgEMGGQLSGGERQRIS 491
Cdd:cd03256 80 IGMIFQQFNLIERlSVLENVlsgRLGrrstwRSLFGLFPKEEKQRALAALERVGLLDKAY-----QRADQLSGGQQQRVA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1805558896 492 IARALLKNAPVVILDEPTAALDIESELAVQKAI--DNLVHNRTVIIIAHRLSTIAGAGN-ILVIEEGQVVEQGTHAQL 566
Cdd:cd03256 155 IARALMQQPKLILADEPVASLDPASSRQVMDLLkrINREEGITVIVSLHQVDLAREYADrIVGLKDGRIVFDGPPAEL 232
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
343-562 |
1.36e-29 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 119.79 E-value: 1.36e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 343 DIRFDNVSYRYeeGDGHALNHVSLTFPAASMSALVGASGAGKTTvtklLMRY-A---DPQQGQISIGGVDIRRLTPEQLN 418
Cdd:COG3839 3 SLELENVSKSY--GGVEALKDIDLDIEDGEFLVLLGPSGCGKST----LLRMiAgleDPTSGEILIGGRDVTDLPPKDRN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 419 slISVVFQDVWLFDD-TLLANI----RIAR-PQATRQE-VEEAARAAQCLEFISRLPqgwltpmgemgGQLSGGERQRIS 491
Cdd:COG3839 77 --IAMVFQSYALYPHmTVYENIafplKLRKvPKAEIDRrVREAAELLGLEDLLDRKP-----------KQLSGGQRQRVA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 492 IARALLKNAPVVILDEPTAALD------IESELA-VQKAIDNlvhnrTVIIIAHRLS---TIagAGNILVIEEGQVVEQG 561
Cdd:COG3839 144 LGRALVREPKVFLLDEPLSNLDaklrveMRAEIKrLHRRLGT-----TTIYVTHDQVeamTL--ADRIAVMNDGRIQQVG 216
|
.
gi 1805558896 562 T 562
Cdd:COG3839 217 T 217
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
344-569 |
2.50e-29 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 116.25 E-value: 2.50e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 344 IRFDNVSYRYeeGDGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRrLTPEQLNSL--- 420
Cdd:COG1126 2 IEIENLHKSF--GDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLT-DSKKDINKLrrk 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 421 ISVVFQDVWLFDD-TLLANIRIArP----QATRQEVEEAARAAqcLE------FISRLPqgwltpmgemgGQLSGGERQR 489
Cdd:COG1126 79 VGMVFQQFNLFPHlTVLENVTLA-PikvkKMSKAEAEERAMEL--LErvgladKADAYP-----------AQLSGGQQQR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 490 ISIARALlknA--PVVIL-DEPTAALDIESELAVQKAIDNLVHN-RTVII----------IAHRlstiagagnILVIEEG 555
Cdd:COG1126 145 VAIARAL---AmePKVMLfDEPTSALDPELVGEVLDVMRDLAKEgMTMVVvthemgfareVADR---------VVFMDGG 212
|
250
....*....|....
gi 1805558896 556 QVVEQGTHAQLLSH 569
Cdd:COG1126 213 RIVEEGPPEEFFEN 226
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
344-569 |
2.59e-29 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 118.64 E-value: 2.59e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 344 IRFDNVSYRYEEGDG--HALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLTPEQLNSL- 420
Cdd:COG1135 2 IELENLSKTFPTKGGpvTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAAr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 421 --ISVVFQDVWLFDD-TLLANI----RIAR-PQATRQEveeaaRAAQCLEFI------SRLPqgwltpmgemgGQLSGGE 486
Cdd:COG1135 82 rkIGMIFQHFNLLSSrTVAENValplEIAGvPKAEIRK-----RVAELLELVglsdkaDAYP-----------SQLSGGQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 487 RQRISIARAlLKNAPVVIL-DEPTAALDIE---SELAVQKAIdnlvhNR----TVIIIAHRLSTI-AGAGNILVIEEGQV 557
Cdd:COG1135 146 KQRVGIARA-LANNPKVLLcDEATSALDPEttrSILDLLKDI-----NRelglTIVLITHEMDVVrRICDRVAVLENGRI 219
|
250
....*....|..
gi 1805558896 558 VEQGTHAQLLSH 569
Cdd:COG1135 220 VEQGPVLDVFAN 231
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
344-566 |
4.24e-29 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 115.92 E-value: 4.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 344 IRFDNVSYRYEEGDgHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLTPEQLNSL--- 420
Cdd:COG3638 3 LELRNLSKRYPGGT-PALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRLrrr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 421 ISVVFQDVWLFDD-TLLANI------RIARPQATRQEV--EEAARAAQCLEFISRLPQGWltpmgEMGGQLSGGERQRIS 491
Cdd:COG3638 82 IGMIFQQFNLVPRlSVLTNVlagrlgRTSTWRSLLGLFppEDRERALEALERVGLADKAY-----QRADQLSGGQQQRVA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1805558896 492 IARALLKNAPVVILDEPTAALDIESELAVQKAIDNLV--HNRTVIIIAHRLSTIAG-AGNILVIEEGQVVEQGTHAQL 566
Cdd:COG3638 157 IARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAreDGITVVVNLHQVDLARRyADRIIGLRDGRVVFDGPPAEL 234
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
344-538 |
1.39e-28 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 113.34 E-value: 1.39e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 344 IRFDNVSYRYEEGDG--HALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLTPEqlnslI 421
Cdd:cd03293 1 LEVRNVSKTYGGGGGavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD-----R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 422 SVVFQDVWLFD-DTLLANIRIARPQATRQEVEEAARAAQCLE------FISRLPqgwltpmgemgGQLSGGERQRISIAR 494
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALGLELQGVPKAEARERAEELLElvglsgFENAYP-----------HQLSGGMRQRVALAR 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1805558896 495 ALLKNAPVVILDEPTAALDIESELAVQKAIDNLV--HNRTVIIIAH 538
Cdd:cd03293 145 ALAVDPDVLLLDEPFSALDALTREQLQEELLDIWreTGKTVLLVTH 190
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
344-568 |
1.82e-28 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 114.48 E-value: 1.82e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 344 IRFDNVSYRYeeGDGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLTPEQLNSLISV 423
Cdd:PRK13548 3 LEARNLSVRL--GGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 424 VFQDVWL-FDDTLLANIRIAR------PQATRQEVEEAARAAQCLEFISRLPQgwltpmgemggQLSGGERQRISIARAL 496
Cdd:PRK13548 81 LPQHSSLsFPFTVEEVVAMGRaphglsRAEDDALVAAALAQVDLAHLAGRDYP-----------QLSGGEQQRVQLARVL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 497 L------KNAPVVILDEPTAALDIESELAVQKAIDNLVHNR--TVIIIAHRLS-TIAGAGNILVIEEGQVVEQGTHAQLL 567
Cdd:PRK13548 150 AqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERglAVIVVLHDLNlAARYADRIVLLHQGRLVADGTPAEVL 229
|
.
gi 1805558896 568 S 568
Cdd:PRK13548 230 T 230
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
359-562 |
3.99e-28 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 113.21 E-value: 3.99e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 359 HALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLTPEQLNSL-ISVVFQDVWLFDD-TLL 436
Cdd:COG0411 18 VAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARLgIARTFQNPRLFPElTVL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 437 ANIRIAR---------------PQATRQEVEEAARAAQCLEFISrlpqgwLTP-MGEMGGQLSGGERQRISIARALLKNA 500
Cdd:COG0411 98 ENVLVAAharlgrgllaallrlPRARREEREARERAEELLERVG------LADrADEPAGNLSYGQQRRLEIARALATEP 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1805558896 501 PVVILDEPTAALDIESELAVQKAIDNL--VHNRTVIIIAHRLSTIAG-AGNILVIEEGQVVEQGT 562
Cdd:COG0411 172 KLLLLDEPAAGLNPEETEELAELIRRLrdERGITILLIEHDMDLVMGlADRIVVLDFGRVIAEGT 236
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
359-569 |
4.18e-28 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 118.63 E-value: 4.18e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 359 HALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRyADPQQGQISIGGVDIRRLTPEQLNSL---ISVVFQD-------- 427
Cdd:COG4172 300 KAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLR-LIPSEGEIRFDGQDLDGLSRRALRPLrrrMQVVFQDpfgslspr 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 428 --VwlfDDTLLANIRIARPQATRQEVEEAARAAqcLE-------FISRLPQgwltpmgemggQLSGGERQRISIARALLK 498
Cdd:COG4172 379 mtV---GQIIAEGLRVHGPGLSAAERRARVAEA--LEevgldpaARHRYPH-----------EFSGGQRQRIAIARALIL 442
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1805558896 499 NAPVVILDEPTAALDieseLAVQKAIDNLV------HNRTVIIIAHRLSTI-AGAGNILVIEEGQVVEQGTHAQLLSH 569
Cdd:COG4172 443 EPKLLVLDEPTSALD----VSVQAQILDLLrdlqreHGLAYLFISHDLAVVrALAHRVMVMKDGKVVEQGPTEQVFDA 516
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
343-562 |
7.37e-28 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 114.81 E-value: 7.37e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 343 DIRFDNVSYRYeeGDGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLmryA---DPQQGQISIGGVDIRRLTPEQLNs 419
Cdd:COG3842 5 ALELENVSKRY--GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMI---AgfeTPDSGRILLDGRDVTGLPPEKRN- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 420 lISVVFQDVWLFDD-TLLANI------RIARPQATRQEVEEAARAAQCLEFISRLPqgwltpmgemgGQLSGGERQRISI 492
Cdd:COG3842 79 -VGMVFQDYALFPHlTVAENVafglrmRGVPKAEIRARVAELLELVGLEGLADRYP-----------HQLSGGQQQRVAL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1805558896 493 ARALLKNAPVVILDEPTAALDIESELAVQKAIDNLVHNR--TVIIIAHRLS---TIagAGNILVIEEGQVVEQGT 562
Cdd:COG3842 147 ARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELgiTFIYVTHDQEealAL--ADRIAVMNDGRIEQVGT 219
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
347-568 |
8.44e-28 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 111.37 E-value: 8.44e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 347 DNVSYRYeeGDGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLTPEQLNSL-ISVVF 425
Cdd:cd03224 4 ENLNAGY--GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAgIGYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 426 QDVWLFDD-TLLANIRIARpqATRQEVEEAARAAQCLEFISRLPQGWltpmGEMGGQLSGGERQRISIARALLKNAPVVI 504
Cdd:cd03224 82 EGRRIFPElTVEENLLLGA--YARRRAKRKARLERVYELFPRLKERR----KQLAGTLSGGEQQMLAIARALMSRPKLLL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 505 LDEPTAAL--DIESElaVQKAIDNLvhNR---TVIIIAHRLSTIAG-AGNILVIEEGQVVEQGTHAQLLS 568
Cdd:cd03224 156 LDEPSEGLapKIVEE--IFEAIREL--RDegvTILLVEQNARFALEiADRAYVLERGRVVLEGTAAELLA 221
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
342-569 |
1.52e-27 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 111.28 E-value: 1.52e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 342 YDIRFDNVSYRYeeGDGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLTPEQLNslI 421
Cdd:cd03296 1 MSIEVRNVSKRF--GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERN--V 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 422 SVVFQDVWLFDD-TLLANIRI---ARPQATRQ-EVEEAARAAQCLEFI------SRLPQgwltpmgemggQLSGGERQRI 490
Cdd:cd03296 77 GFVFQHYALFRHmTVFDNVAFglrVKPRSERPpEAEIRAKVHELLKLVqldwlaDRYPA-----------QLSGGQRQRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 491 SIARALLKNAPVVILDEPTAALD--IESEL-AVQKAIDNLVHNRTVIIIAHRLSTIAGAGNILVIEEGQVVEQGTHAQLL 567
Cdd:cd03296 146 ALARALAVEPKVLLLDEPFGALDakVRKELrRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVY 225
|
..
gi 1805558896 568 SH 569
Cdd:cd03296 226 DH 227
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
23-573 |
2.09e-27 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 118.12 E-value: 2.09e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 23 VGSQARMLRRSMLALLLAAFMQGIAFACLYPIIDALLRGDAPQLL-------------NW------AMAFSVAAIVTLVL 83
Cdd:TIGR00957 296 VKSPHKPRKPSLFKVLYKTFGPYFLMSFCFKAIHDLMMFIGPQILsllirfvndpmapDWqgyfytGLLFVCACLQTLIL 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 84 RWYG-----LGFEYRGHLAQATHELRLRLGEQLRRVpleklqrGRAGEMNALLlgSVDENlnYVIAIANILLLTIVTPLT 158
Cdd:TIGR00957 376 HQYFhicfvSGMRIKTAVMGAVYRKALVITNSARKS-------STVGEIVNLM--SVDAQ--RFMDLATYINMIWSAPLQ 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 159 ASLATLWIDWRLG-------LVMLLIFPLlvpfyywrRPAMRRQMQTLGEAHQRLSGDIV----EFAQGMMVLRTCGSD- 226
Cdd:TIGR00957 445 VILALYFLWLNLGpsvlagvAVMVLMVPL--------NAVMAMKTKTYQVAHMKSKDNRIklmnEILNGIKVLKLYAWEl 516
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 227 ADKSRALLAHFNALENLQTRTHRQGAGATMLIASvvelGLQVVVLSGIVWVVTGTLNL-----AFLIAAVAMIMRFaePM 301
Cdd:TIGR00957 517 AFLDKVEGIRQEELKVLKKSAYLHAVGTFTWVCT----PFLVALITFAVYVTVDENNIldaekAFVSLALFNILRF--PL 590
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 302 AMFISYTSVVELIASALQRIERFMA---IAPLPVAEQSEMP-ERYDIRFDNVSYRYEEGDGHALNHVSLTFPAASMSALV 377
Cdd:TIGR00957 591 NILPMVISSIVQASVSLKRLRIFLSheeLEPDSIERRTIKPgEGNSITVHNATFTWARDLPPTLNGITFSIPEGALVAVV 670
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 378 GASGAGKTTVTKLLMRYADPQQGQISIGGVdirrltpeqlnslISVVFQDVWLFDDTLLANIRIARP--QATRQEVEEAA 455
Cdd:TIGR00957 671 GQVGCGKSSLLSALLAEMDKVEGHVHMKGS-------------VAYVPQQAWIQNDSLRENILFGKAlnEKYYQQVLEAC 737
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 456 RAAQCLEFisrLPQGWLTPMGEMGGQLSGGERQRISIARALLKNAPVVILDEPTAALDIEselaVQKAI-------DNLV 528
Cdd:TIGR00957 738 ALLPDLEI---LPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAH----VGKHIfehvigpEGVL 810
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 1805558896 529 HNRTVIIIAHRLSTIAGAGNILVIEEGQVVEQGTHAQLLSHHGRY 573
Cdd:TIGR00957 811 KNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAF 855
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
344-568 |
2.30e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 111.80 E-value: 2.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 344 IRFDNVSYRYEEG---DGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLTPE----Q 416
Cdd:PRK13646 3 IRFDNVSYTYQKGtpyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDkyirP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 417 LNSLISVVFQ--DVWLFDDTLLANIrIARPQATRQEVEEA-ARAAQCL-EF-ISRlpqgwlTPMGEMGGQLSGGERQRIS 491
Cdd:PRK13646 83 VRKRIGMVFQfpESQLFEDTVEREI-IFGPKNFKMNLDEVkNYAHRLLmDLgFSR------DVMSQSPFQMSGGQMRKIA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 492 IARALLKNAPVVILDEPTAALDIESELAVQKAIDNLV--HNRTVIIIAHRLSTIAG-AGNILVIEEGQVVEQGTHAQLLS 568
Cdd:PRK13646 156 IVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtdENKTIILVSHDMNEVARyADEVIVMKEGSIVSQTSPKELFK 235
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
344-538 |
2.61e-27 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 109.80 E-value: 2.61e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 344 IRFDNVSYRYEeGDGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLTPEQLNSL--- 420
Cdd:cd03292 1 IEFINVTKTYP-NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLrrk 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 421 ISVVFQDVWLFDD-TLLANIRIARP--QATRQEVEEaaRAAQCLEFIsrlpqGWLTPMGEMGGQLSGGERQRISIARALL 497
Cdd:cd03292 80 IGVVFQDFRLLPDrNVYENVAFALEvtGVPPREIRK--RVPAALELV-----GLSHKHRALPAELSGGEQQRVAIARAIV 152
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1805558896 498 KNAPVVILDEPTAALDIESELAVQKaIDNLVHNR--TVIIIAH 538
Cdd:cd03292 153 NSPTILIADEPTGNLDPDTTWEIMN-LLKKINKAgtTVVVATH 194
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
344-569 |
2.97e-27 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 111.65 E-value: 2.97e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 344 IRFDNVSYRYEEGDGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGV--------DIRRltpe 415
Cdd:PRK13635 6 IRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMvlseetvwDVRR---- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 416 qlnsLISVVFQD-------VWLFDDTL--LANIRIARPQATRQeVEEAARAAQCLEFISRLPQgwltpmgemggQLSGGE 486
Cdd:PRK13635 82 ----QVGMVFQNpdnqfvgATVQDDVAfgLENIGVPREEMVER-VDQALRQVGMEDFLNREPH-----------RLSGGQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 487 RQRISIARALLKNAPVVILDEPTAALDIESELAVQKAIDNLVHNR--TVIIIAHRLSTIAGAGNILVIEEGQVVEQGTHA 564
Cdd:PRK13635 146 KQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKgiTVLSITHDLDEAAQADRVIVMNKGEILEEGTPE 225
|
....*
gi 1805558896 565 QLLSH 569
Cdd:PRK13635 226 EIFKS 230
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
359-576 |
1.12e-26 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 110.98 E-value: 1.12e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 359 HALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLTPEQLNSL---ISVVFQD-------- 427
Cdd:COG4608 32 KAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRPLrrrMQMVFQDpyaslnpr 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 428 --VwlfDDTLLANIRIARpQATRQEVEEaaRAAQCL-------EFISRLPQgwltpmgemggQLSGGERQRISIARALLK 498
Cdd:COG4608 112 mtV---GDIIAEPLRIHG-LASKAERRE--RVAELLelvglrpEHADRYPH-----------EFSGGQRQRIGIARALAL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 499 NAPVVILDEPTAALDIeselAVQKAIDNLV------HNRTVIIIAHRLST---IagAGNILVIEEGQVVEQGTHAQLLSH 569
Cdd:COG4608 175 NPKLIVCDEPVSALDV----SIQAQVLNLLedlqdeLGLTYLFISHDLSVvrhI--SDRVAVMYLGKIVEIAPRDELYAR 248
|
....*....
gi 1805558896 570 --HGRYQAL 576
Cdd:COG4608 249 plHPYTQAL 257
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
345-558 |
1.23e-26 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 107.73 E-value: 1.23e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 345 RFDNVSYRYEEGdGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRltpEQLNSLISVV 424
Cdd:cd03226 1 RIENISFSYKKG-TEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKA---KERRKSIGYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 425 FQDV--WLFDDTLLANIRIARPQATR--QEVEEAARAAQCLEFISRLPQgwltpmgemggQLSGGERQRISIARALLKNA 500
Cdd:cd03226 77 MQDVdyQLFTDSVREELLLGLKELDAgnEQAETVLKDLDLYALKERHPL-----------SLSGGQKQRLAIAAALLSGK 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 501 PVVILDEPTAALDIESELAVQKAIDNLV-HNRTVIIIAHRLSTIAGAGNILV-IEEGQVV 558
Cdd:cd03226 146 DLLIFDEPTSGLDYKNMERVGELIRELAaQGKAVIVITHDYEFLAKVCDRVLlLANGAIV 205
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
344-558 |
3.28e-26 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 104.82 E-value: 3.28e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 344 IRFDNVSYRYeeGDGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLTP-EQLNSLIS 422
Cdd:cd03216 1 LELRGITKRF--GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPrDARRAGIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 423 VVFQdvwlfddtllaniriarpqatrqeveeaaraaqclefisrlpqgwltpmgemggqLSGGERQRISIARALLKNAPV 502
Cdd:cd03216 79 MVYQ-------------------------------------------------------LSVGERQMVEIARALARNARL 103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1805558896 503 VILDEPTAALDIESELAVQKAIDNLV-HNRTVIIIAHRLSTI-AGAGNILVIEEGQVV 558
Cdd:cd03216 104 LILDEPTAALTPAEVERLFKVIRRLRaQGVAVIFISHRLDEVfEIADRVTVLRDGRVV 161
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
344-561 |
7.07e-26 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 105.80 E-value: 7.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 344 IRFDNVSYRYeeGDGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLTPEQLNslISV 423
Cdd:cd03301 1 VELENVTKRF--GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRD--IAM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 424 VFQDVWLFDD-TLLANI------RIARPQATRQEVEEAARAAQCLEFISRLPQgwltpmgemggQLSGGERQRISIARAL 496
Cdd:cd03301 77 VFQNYALYPHmTVYDNIafglklRKVPKDEIDERVREVAELLQIEHLLDRKPK-----------QLSGGQRQRVALGRAI 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1805558896 497 LKNAPVVILDEPTAALDIESELAVQKAIDNL--VHNRTVIIIAH-RLSTIAGAGNILVIEEGQVVEQG 561
Cdd:cd03301 146 VREPKVFLMDEPLSNLDAKLRVQMRAELKRLqqRLGTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
343-569 |
2.17e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 106.26 E-value: 2.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 343 DIRFDNVSYRYEEG---DGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGvdiRRLTPE---- 415
Cdd:PRK13634 2 DITFQKVEHRYQYKtpfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGE---RVITAGkknk 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 416 QLNSL---ISVVFQ--DVWLFDDTLLANIRIArPQATRQEVEEA-ARAAQCLEFISrLPQGWLT--PMgemggQLSGGER 487
Cdd:PRK13634 79 KLKPLrkkVGIVFQfpEHQLFEETVEKDICFG-PMNFGVSEEDAkQKAREMIELVG-LPEELLArsPF-----ELSGGQM 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 488 QRISIARALLKNAPVVILDEPTAALDIESELAVQKAIDNL--VHNRTVIIIAHRLSTIAG-AGNILVIEEGQVVEQGTHA 564
Cdd:PRK13634 152 RRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLhkEKGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPR 231
|
....*
gi 1805558896 565 QLLSH 569
Cdd:PRK13634 232 EIFAD 236
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
344-566 |
2.38e-25 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 104.12 E-value: 2.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 344 IRFDNVSYRYEEGDGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRlTPEQLNSLISV 423
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 424 VFQDVWLFDD-TLLANIRI-ARPQA--TRQEVEEAARAAQCLEfisrLPQGWLTPMGemggQLSGGERQRISIARALLKN 499
Cdd:cd03263 80 CPQFDALFDElTVREHLRFyARLKGlpKSEIKEEVELLLRVLG----LTDKANKRAR----TLSGGMKRKLSLAIALIGG 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1805558896 500 APVVILDEPTAALDIESELAVQKAIDNLVHNRTVIIIAH------RLSTiagagNILVIEEGQVVEQGTHAQL 566
Cdd:cd03263 152 PSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHsmdeaeALCD-----RIAIMSDGKLRCIGSPQEL 219
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
344-538 |
3.77e-25 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 103.38 E-value: 3.77e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 344 IRFDNVSYRYeeGDGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRrLTPEQLNSL--- 420
Cdd:cd03262 1 IEIKNLHKSF--GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLT-DDKKNINELrqk 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 421 ISVVFQDVWLFDD-TLLANIRIARPQATRQEVEEA-ARAAQCLEFISRLPQGWLTPmgemgGQLSGGERQRISIARALLK 498
Cdd:cd03262 78 VGMVFQQFNLFPHlTVLENITLAPIKVKGMSKAEAeERALELLEKVGLADKADAYP-----AQLSGGQQQRVAIARALAM 152
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1805558896 499 NAPVVILDEPTAALDIESELAVQKAIDNLVH-NRTVIIIAH 538
Cdd:cd03262 153 NPKVMLFDEPTSALDPELVGEVLDVMKDLAEeGMTMVVVTH 193
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
344-568 |
6.40e-25 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 104.50 E-value: 6.40e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 344 IRFDNVSYRYEEG-----DGHA--LNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLTPEQ 416
Cdd:TIGR02769 3 LEVRDVTHTYRTGglfgaKQRApvLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 417 LNSL---ISVVFQDVW-LFDDTLLANIRIARPQATRQEVEEAARAAQCLEFIS----------RLPQgwltpmgemggQL 482
Cdd:TIGR02769 83 RRAFrrdVQLVFQDSPsAVNPRMTVRQIIGEPLRHLTSLDESEQKARIAELLDmvglrsedadKLPR-----------QL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 483 SGGERQRISIARALLKNAPVVILDEPTAALDIESELAVQKAIDNLVH--NRTVIIIAHRLSTIAG-AGNILVIEEGQVVE 559
Cdd:TIGR02769 152 SGGQLQRINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQafGTAYLFITHDLRLVQSfCQRVAVMDKGQIVE 231
|
....*....
gi 1805558896 560 QGTHAQLLS 568
Cdd:TIGR02769 232 ECDVAQLLS 240
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
344-570 |
9.11e-25 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 103.12 E-value: 9.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 344 IRFDNVSYRYEegdgHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLTPEQlnSLISV 423
Cdd:PRK10771 2 LKLTDITWLYH----HLPMRFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSR--RPVSM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 424 VFQDVWLFDD-TLLANI--------RIARPQatRQEVEEAARAAQCLEFISRLPqgwltpmgemgGQLSGGERQRISIAR 494
Cdd:PRK10771 76 LFQENNLFSHlTVAQNIglglnpglKLNAAQ--REKLHAIARQMGIEDLLARLP-----------GQLSGGQRQRVALAR 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1805558896 495 ALLKNAPVVILDEPTAALDIESELAVQKAIDNLVHNR--TVIIIAHRLSTIAG-AGNILVIEEGQVVEQGTHAQLLSHH 570
Cdd:PRK10771 143 CLVREQPILLLDEPFSALDPALRQEMLTLVSQVCQERqlTLLMVSHSLEDAARiAPRSLVVADGRIAWDGPTDELLSGK 221
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
344-569 |
1.28e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 103.68 E-value: 1.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 344 IRFDNVSYRYEEGDGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLTPEQLNSLISV 423
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 424 VFQD--------VWLFDDTL-LANIRIARPQATRqEVEEAARAAQCLEFISRLPQGwltpmgemggqLSGGERQRISIAR 494
Cdd:PRK13648 88 VFQNpdnqfvgsIVKYDVAFgLENHAVPYDEMHR-RVSEALKQVDMLERADYEPNA-----------LSGGQKQRVAIAG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 495 ALLKNAPVVILDEPTAALDIESelavQKAIDNLVH------NRTVIIIAHRLSTIAGAGNILVIEEGQVVEQGTHAQLLS 568
Cdd:PRK13648 156 VLALNPSVIILDEATSMLDPDA----RQNLLDLVRkvksehNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFD 231
|
.
gi 1805558896 569 H 569
Cdd:PRK13648 232 H 232
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
344-546 |
1.52e-24 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 101.40 E-value: 1.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 344 IRFDNVSYRYeeGDGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLtPEQLNSLISV 423
Cdd:COG4133 3 LEAENLSCRR--GERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDA-REDYRRRLAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 424 VFQDVWLFDD-TLLANIRIAR----PQATRQEVEEAARAAQCLEFISRLPqgwltpmgemgGQLSGGERQRISIARALLK 498
Cdd:COG4133 80 LGHADGLKPElTVRENLRFWAalygLRADREAIDEALEAVGLAGLADLPV-----------RQLSAGQKRRVALARLLLS 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1805558896 499 NAPVVILDEPTAALDIESELAVQKAIDNLVHNRTVIIIA-HRLSTIAGA 546
Cdd:COG4133 149 PAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTtHQPLELAAA 197
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
344-561 |
1.69e-24 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 101.09 E-value: 1.69e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 344 IRFDNVSYRYEEGDGHA----LNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQ--GQISIGGvdiRRLTPEQL 417
Cdd:cd03213 4 LSFRNLTVTVKSSPSKSgkqlLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGvsGEVLING---RPLDKRSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 418 NSLISVVFQDvwlfdDTLLaniriarPQATrqeVEEAaraaqcLEFISRLpQGwltpmgemggqLSGGERQRISIARALL 497
Cdd:cd03213 81 RKIIGYVPQD-----DILH-------PTLT---VRET------LMFAAKL-RG-----------LSGGERKRVSIALELV 127
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1805558896 498 KNAPVVILDEPTAALDIESELAVQKAIDNLVH-NRTVIIIAHRLST--IAGAGNILVIEEGQVVEQG 561
Cdd:cd03213 128 SNPSLLFLDEPTSGLDSSSALQVMSLLRRLADtGRTIICSIHQPSSeiFELFDKLLLLSQGRVIYFG 194
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
344-561 |
2.70e-24 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 101.09 E-value: 2.70e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 344 IRFDNVSYRYEegdgHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLTPEQlnSLISV 423
Cdd:TIGR01277 1 LALDKVRYEYE----HLPMEFDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQ--RPVSM 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 424 VFQDVWLFDD-TLLANIRIA-----RPQATRQE-VEEAARAAQCLEFISRLPqgwltpmgemgGQLSGGERQRISIARAL 496
Cdd:TIGR01277 75 LFQENNLFAHlTVRQNIGLGlhpglKLNAEQQEkVVDAAQQVGIADYLDRLP-----------EQLSGGQRQRVALARCL 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 497 LKNAPVVILDEPTAALD----IESELAVQKAIDNlvHNRTVIIIAHRLSTIAG-AGNILVIEEGQVVEQG 561
Cdd:TIGR01277 144 VRPNPILLLDEPFSALDpllrEEMLALVKQLCSE--RQRTLLMVTHHLSDARAiASQIAVVSQGKIKVVS 211
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
375-569 |
3.00e-24 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 101.64 E-value: 3.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 375 ALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLTPEQLNslISVVFQDVWLFDD-TLLANI-------RIARPQA 446
Cdd:cd03299 29 VILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRD--ISYVPQNYALFPHmTVYKNIayglkkrKVDKKEI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 447 TRqEVEEAARAAQCLEFISRLPqgwltpmgemgGQLSGGERQRISIARALLKNAPVVILDEPTAALDIESELAVQKAIDN 526
Cdd:cd03299 107 ER-KVLEIAEMLGIDHLLNRKP-----------ETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELKK 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1805558896 527 LVHNR--TVIIIAHRLSTIAGAGN-ILVIEEGQVVEQGTHAQLLSH 569
Cdd:cd03299 175 IRKEFgvTVLHVTHDFEEAWALADkVAIMLNGKLIQVGKPEEVFKK 220
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
357-575 |
3.31e-24 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 104.92 E-value: 3.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 357 DG-HALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLTPEQlnSLISVVFQDVWLFDD-T 434
Cdd:PRK11607 30 DGqHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQ--RPINMMFQSYALFPHmT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 435 LLANIRIARPQATRQEVEEAARAAQCL------EFISRLPQgwltpmgemggQLSGGERQRISIARALLKNAPVVILDEP 508
Cdd:PRK11607 108 VEQNIAFGLKQDKLPKAEIASRVNEMLglvhmqEFAKRKPH-----------QLSGGQRQRVALARSLAKRPKLLLLDEP 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1805558896 509 TAALDIESELAVQKAIDNLVH--NRTVIIIAH-RLSTIAGAGNILVIEEGQVVEQGTHAQLLSH-HGRYQA 575
Cdd:PRK11607 177 MGALDKKLRDRMQLEVVDILErvGVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHpTTRYSA 247
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
344-569 |
5.03e-24 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 103.69 E-value: 5.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 344 IRFDNVSYRYeeGDGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLmryA---DPQQGQISIGGVDIR-RLTPEQLNs 419
Cdd:COG1118 3 IEVRNISKRF--GSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRII---AgleTPDSGRIVLNGRDLFtNLPPRERR- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 420 lISVVFQDVWLFDD-TLLANI----RIARP--QATRQEVEEAARAAQCLEFISRLPqgwltpmgemgGQLSGGERQRISI 492
Cdd:COG1118 77 -VGFVFQHYALFPHmTVAENIafglRVRPPskAEIRARVEELLELVQLEGLADRYP-----------SQLSGGQRQRVAL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 493 ARALLKNAPVVILDEPTAALDIeselAVQKAI-DNLVH-----NRTVIIIAH------RLstiagAGNILVIEEGQVVEQ 560
Cdd:COG1118 145 ARALAVEPEVLLLDEPFGALDA----KVRKELrRWLRRlhdelGGTTVFVTHdqeealEL-----ADRVVVMNQGRIEQV 215
|
....*....
gi 1805558896 561 GTHAQLLSH 569
Cdd:COG1118 216 GTPDEVYDR 224
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
359-566 |
8.00e-24 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 105.10 E-value: 8.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 359 HALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLTPEQLNSL-ISVVFQDVWLFDD-TLL 436
Cdd:COG1129 18 KALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAgIAIIHQELNLVPNlSVA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 437 ANIRIARPQATRQEVEEAARAAQCLEFISRL-----PQgwlTPMGEmggqLSGGERQRISIARALLKNAPVVILDEPTAA 511
Cdd:COG1129 98 ENIFLGREPRRGGLIDWRAMRRRARELLARLgldidPD---TPVGD----LSVAQQQLVEIARALSRDARVLILDEPTAS 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 512 LDiESElaVQ---KAIDNLV-HNRTVIIIAHRLSTIAG-AGNILVIEEGQVVEQGTHAQL 566
Cdd:COG1129 171 LT-ERE--VErlfRIIRRLKaQGVAIIYISHRLDEVFEiADRVTVLRDGRLVGTGPVAEL 227
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
344-561 |
1.23e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 100.97 E-value: 1.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 344 IRFDNVSYRYEEGDgHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLTPEQLNSLISV 423
Cdd:PRK13647 5 IEVEDLHFRYKDGT-KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 424 VFQD---------VWlfDDTLLA--NIRIARPQATRQeVEEAARAAQCLEFISRLPQgwltpmgemggQLSGGERQRISI 492
Cdd:PRK13647 84 VFQDpddqvfsstVW--DDVAFGpvNMGLDKDEVERR-VEEALKAVRMWDFRDKPPY-----------HLSYGQKKRVAI 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1805558896 493 ARALLKNAPVVILDEPTAALDIESELAVQKAIDNLvHNR--TVIIIAHRLSTIAG-AGNILVIEEGQVVEQG 561
Cdd:PRK13647 150 AGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRL-HNQgkTVIVATHDVDLAAEwADQVIVLKEGRVLAEG 220
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
348-569 |
1.27e-23 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 99.67 E-value: 1.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 348 NVSYryeeGDGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLTPEQLNSL-ISVVFQ 426
Cdd:COG0410 10 HAGY----GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLgIGYVPE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 427 DVWLFDD-TLLANIRIARpQATRQEVEEAARAAQCLEFISRLpqgwltpmGEM----GGQLSGGERQRISIARALLKNAP 501
Cdd:COG0410 86 GRRIFPSlTVEENLLLGA-YARRDRAEVRADLERVYELFPRL--------KERrrqrAGTLSGGEQQMLAIGRALMSRPK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 502 VVILDEPTAALdieSELAVQKAIDNLVH-NR---TVII----------IAHRlstiagagnILVIEEGQVVEQGTHAQLL 567
Cdd:COG0410 157 LLLLDEPSLGL---APLIVEEIFEIIRRlNRegvTILLveqnarfaleIADR---------AYVLERGRIVLEGTAAELL 224
|
..
gi 1805558896 568 SH 569
Cdd:COG0410 225 AD 226
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
357-561 |
1.48e-23 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 98.91 E-value: 1.48e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 357 DGHALNhVSLTFPAaSMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGV---DIRR---LTPEQLNslISVVFQDVWL 430
Cdd:cd03297 11 PDFTLK-IDFDLNE-EVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfDSRKkinLPPQQRK--IGLVFQQYAL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 431 FDD-TLLANI----RIARPQATRQEVEEAARAAQCLEFISRLPQgwltpmgemggQLSGGERQRISIARALLKNAPVVIL 505
Cdd:cd03297 87 FPHlNVRENLafglKRKRNREDRISVDELLDLLGLDHLLNRYPA-----------QLSGGEKQRVALARALAAQPELLLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1805558896 506 DEPTAALDIESELAVQKAIDNLVH--NRTVIIIAHRLSTIAG-AGNILVIEEGQVVEQG 561
Cdd:cd03297 156 DEPFSALDRALRLQLLPELKQIKKnlNIPVIFVTHDLSEAEYlADRIVVMEDGRLQYIG 214
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
344-566 |
1.54e-23 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 98.98 E-value: 1.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 344 IRFDNVSYRYeeGDGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRlTPEQLNSLISV 423
Cdd:cd03265 1 IEVENLVKKY--GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 424 VFQDVWLfDDTLLA--NIRI-ARPQATRQEvEEAARAAQCLEFIsrlpqGWLTPMGEMGGQLSGGERQRISIARALLKNA 500
Cdd:cd03265 78 VFQDLSV-DDELTGweNLYIhARLYGVPGA-ERRERIDELLDFV-----GLLEAADRLVKTYSGGMRRRLEIARSLVHRP 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1805558896 501 PVVILDEPTAALDIESELAVQKAIDNLV--HNRTVIIIAHRLSTI-AGAGNILVIEEGQVVEQGTHAQL 566
Cdd:cd03265 151 EVLFLDEPTIGLDPQTRAHVWEYIEKLKeeFGMTILLTTHYMEEAeQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
343-570 |
2.30e-23 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 99.70 E-value: 2.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 343 DIRFDNVSYRYeeGDGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLTPEQLNSLIS 422
Cdd:PRK11231 2 TLRTENLTVGY--GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 423 VVFQDV------------------WLfddTLLAniRIArpQATRQEVEEAARAAQCLEFISRLpqgwLTpmgemggQLSG 484
Cdd:PRK11231 80 LLPQHHltpegitvrelvaygrspWL---SLWG--RLS--AEDNARVNQAMEQTRINHLADRR----LT-------DLSG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 485 GERQRISIARALLKNAPVVILDEPTAALDIESELAVQKAIDNLVHN-RTVIIIAHRLSTIAG-AGNILVIEEGQVVEQGT 562
Cdd:PRK11231 142 GQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQgKTVVTVLHDLNQASRyCDHLVVLANGHVMAQGT 221
|
....*...
gi 1805558896 563 HAQLLSHH 570
Cdd:PRK11231 222 PEEVMTPG 229
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
344-562 |
9.80e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 98.65 E-value: 9.80e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 344 IRFDNVSYRYEEGD---GHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLTPEQ---- 416
Cdd:PRK13643 2 IKFEKVNYTYQPNSpfaSRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKeikp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 417 LNSLISVVFQ--DVWLFDDTLLANIRIArPQATRQEVEEAAR-AAQCLEFISRLPQGW-LTPMgemggQLSGGERQRISI 492
Cdd:PRK13643 82 VRKKVGVVFQfpESQLFEETVLKDVAFG-PQNFGIPKEKAEKiAAEKLEMVGLADEFWeKSPF-----ELSGGQMRRVAI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1805558896 493 ARALLKNAPVVILDEPTAALDIESELAVQKAIDNLVHN-RTVIIIAHRLSTIAG-AGNILVIEEGQVVEQGT 562
Cdd:PRK13643 156 AGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSgQTVVLVTHLMDDVADyADYVYLLEKGHIISCGT 227
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
344-567 |
1.17e-22 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 97.46 E-value: 1.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 344 IRFDNVSYRYeeGDGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLTPEQLNSLISV 423
Cdd:COG4604 2 IEIKNVSKRY--GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 424 VFQDVWLfddtllaNIRI---------------ARP-QATRQEVEEAaraaqcLEFISrlpqgwLTPM-GEMGGQLSGGE 486
Cdd:COG4604 80 LRQENHI-------NSRLtvrelvafgrfpyskGRLtAEDREIIDEA------IAYLD------LEDLaDRYLDELSGGQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 487 RQRISIARALLKNAPVVILDEPTAALDIESELAVQKAIDNLV--HNRTVIIIAHRLSTIAG-AGNILVIEEGQVVEQGTH 563
Cdd:COG4604 141 RQRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLAdeLGKTVVIVLHDINFASCyADHIVAMKDGRVVAQGTP 220
|
....
gi 1805558896 564 AQLL 567
Cdd:COG4604 221 EEII 224
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
344-559 |
1.34e-22 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 96.65 E-value: 1.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 344 IRFDNVSYRYEEG--DGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLTPEQLNSL- 420
Cdd:TIGR02211 2 LKCENLGKRYQEGklDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERAKLr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 421 ---ISVVFQDVWLFDD-TLLANIriARPQ-ATRQEVEEAARAAQclEFISRLpqGWLTPMGEMGGQLSGGERQRISIARA 495
Cdd:TIGR02211 82 nkkLGFIYQFHHLLPDfTALENV--AMPLlIGKKSVKEAKERAY--EMLEKV--GLEHRINHRPSELSGGERQRVAIARA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1805558896 496 LLKNAPVVILDEPTAALDIESELAVQKAID--NLVHNRTVIIIAHRLSTIAGAGNILVIEEGQVVE 559
Cdd:TIGR02211 156 LVNQPSLVLADEPTGNLDNNNAKIIFDLMLelNRELNTSFLVVTHDLELAKKLDRVLEMKDGQLFN 221
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
360-569 |
1.39e-22 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 97.71 E-value: 1.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 360 ALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLTPEQLNSL----ISVVFQDVWLFDD-T 434
Cdd:cd03294 39 GVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELrrkkISMVFQSFALLPHrT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 435 LLANIRIARPQATRQEVEEAARAAQCLEFISrlpqgwLTPMGE-MGGQLSGGERQRISIARALLKNAPVVILDEPTAALD 513
Cdd:cd03294 119 VLENVAFGLEVQGVPRAEREERAAEALELVG------LEGWEHkYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALD 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1805558896 514 --IESE-----LAVQKAidnlvHNRTVIIIAHRLSTIAGAGN-ILVIEEGQVVEQGTHAQLLSH 569
Cdd:cd03294 193 plIRREmqdelLRLQAE-----LQKTIVFITHDLDEALRLGDrIAIMKDGRLVQVGTPEEILTN 251
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
358-568 |
1.79e-22 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 99.03 E-value: 1.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 358 GHALNhVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGV---DIRR---LTPEQlnSLISVVFQDVWLF 431
Cdd:TIGR02142 11 DFSLD-ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRtlfDSRKgifLPPEK--RRIGYVFQEARLF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 432 D-----DTLLANIRIARPQATRQEVEEAARAAQCLEFISRLPqgwltpmgemgGQLSGGERQRISIARALLKNAPVVILD 506
Cdd:TIGR02142 88 PhlsvrGNLRYGMKRARPSERRISFERVIELLGIGHLLGRLP-----------GRLSGGEKQRVAIGRALLSSPRLLLMD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1805558896 507 EPTAALDIESELAVQKAIDNLVH--NRTVIIIAHRLSTIAG-AGNILVIEEGQVVEQGTHAQLLS 568
Cdd:TIGR02142 157 EPLAALDDPRKYEILPYLERLHAefGIPILYVSHSLQEVLRlADRVVVLEDGRVAAAGPIAEVWA 221
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
344-569 |
2.28e-22 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 96.24 E-value: 2.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 344 IRFDNVSYRYeeGDGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDI---RRLTPEQLNSL 420
Cdd:COG4161 3 IQLKNINCFY--GSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsQKPSEKAIRLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 421 ---ISVVFQDVWLFDD-TLLANIRIARPQATRQEVEEA-ARAAQCL------EFISRLPQgwltpmgemggQLSGGERQR 489
Cdd:COG4161 81 rqkVGMVFQQYNLWPHlTVMENLIEAPCKVLGLSKEQArEKAMKLLarlrltDKADRFPL-----------HLSGGQQQR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 490 ISIARALLKNAPVVILDEPTAALDIESELAVQKAIDNLVHNR-TVIIIAHRLStIAG--AGNILVIEEGQVVEQGTH--- 563
Cdd:COG4161 150 VAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGiTQVIVTHEVE-FARkvASQVVYMEKGRIIEQGDAshf 228
|
250
....*....|....
gi 1805558896 564 --------AQLLSH 569
Cdd:COG4161 229 tqpqteafAHYLSH 242
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
344-569 |
2.50e-22 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 96.24 E-value: 2.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 344 IRFDNVSYRYeeGDGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGG--VDIRRLTPE----QL 417
Cdd:PRK11124 3 IQLNGINCFY--GAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhFDFSKTPSDkairEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 418 NSLISVVFQ--DVW----LFDDTLLANIRI---ARPQATRQEVEEAARAaQCLEFISRLPQgwltpmgemggQLSGGERQ 488
Cdd:PRK11124 81 RRNVGMVFQqyNLWphltVQQNLIEAPCRVlglSKDQALARAEKLLERL-RLKPYADRFPL-----------HLSGGQQQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 489 RISIARALLKNAPVVILDEPTAALDIESELAVQKAIDNLVHNR-TVIIIAHRLStIAG--AGNILVIEEGQVVEQGTH-- 563
Cdd:PRK11124 149 RVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGiTQVIVTHEVE-VARktASRVVYMENGHIVEQGDAsc 227
|
250
....*....|....*
gi 1805558896 564 ---------AQLLSH 569
Cdd:PRK11124 228 ftqpqteafKNYLSH 242
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
344-569 |
2.82e-22 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 98.33 E-value: 2.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 344 IRFDNVSYRYEEGDG--HALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLTPEQLNSL- 420
Cdd:PRK11153 2 IELKNISKVFPQGGRtiHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKAr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 421 --ISVVFQDVWL------FDDTLLAnIRIARpqATRQEVEeaARAAQCLEFI------SRLPqgwltpmgemgGQLSGGE 486
Cdd:PRK11153 82 rqIGMIFQHFNLlssrtvFDNVALP-LELAG--TPKAEIK--ARVTELLELVglsdkaDRYP-----------AQLSGGQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 487 RQRISIARAlLKNAPVVIL-DEPTAALDIE---SELAVQKAIdnlvhNR----TVIIIAHRLSTIAG-AGNILVIEEGQV 557
Cdd:PRK11153 146 KQRVAIARA-LASNPKVLLcDEATSALDPAttrSILELLKDI-----NRelglTIVLITHEMDVVKRiCDRVAVIDAGRL 219
|
250
....*....|..
gi 1805558896 558 VEQGTHAQLLSH 569
Cdd:PRK11153 220 VEQGTVSEVFSH 231
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
344-562 |
3.83e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 96.79 E-value: 3.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 344 IRFDNVSYRYEEGDGHALNHVSLTFPAASMSALVGASGAGKTTVTKL---LMRYADPQQGQISIGGVDIRRLTPEQLNSL 420
Cdd:PRK13640 6 VEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLingLLLPDDNPNSKITVDGITLTAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 421 ISVVFQD-------VWLFDDTL--LANIRIARPQATRQeVEEAARAAQCLEFISRLPQgwltpmgemggQLSGGERQRIS 491
Cdd:PRK13640 86 VGIVFQNpdnqfvgATVGDDVAfgLENRAVPRPEMIKI-VRDVLADVGMLDYIDSEPA-----------NLSGGQKQRVA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1805558896 492 IARALLKNAPVVILDEPTAALDIESELAVQKAIDNLV--HNRTVIIIAHRLSTIAGAGNILVIEEGQVVEQGT 562
Cdd:PRK13640 154 IAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKkkNNLTVISITHDIDEANMADQVLVLDDGKLLAQGS 226
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
344-567 |
5.76e-22 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 95.54 E-value: 5.76e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 344 IRFDNVSYRYeeGDGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQ-ISI-----GGVDIRRLTP--- 414
Cdd:COG1119 4 LELRNVTVRR--GGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLfgerrGGEDVWELRKrig 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 415 -------EQLNSLISVvfQDVWL--FDDTllanirIARPQATrqEVEEAARAAQCLEF--ISRLPQgwlTPMGemggQLS 483
Cdd:COG1119 82 lvspalqLRFPRDETV--LDVVLsgFFDS------IGLYREP--TDEQRERARELLELlgLAHLAD---RPFG----TLS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 484 GGERQRISIARALLKNAPVVILDEPTAALDIESELAVQKAIDNLVHN--RTVIIIAHRLSTI-AGAGNILVIEEGQVVEQ 560
Cdd:COG1119 145 QGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEgaPTLVLVTHHVEEIpPGITHVLLLKDGRVVAA 224
|
....*..
gi 1805558896 561 GTHAQLL 567
Cdd:COG1119 225 GPKEEVL 231
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
361-569 |
6.01e-22 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 95.20 E-value: 6.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 361 LNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDI---RRLTPEQ-----LNSLISVVFQDVWLFD 432
Cdd:PRK11264 19 LHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdtaRSLSQQKglirqLRQHVGFVFQNFNLFP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 433 D-TLLANIrIARPQATRQEVEEAARAaqclefisrLPQGWLTPMGEMGGQ------LSGGERQRISIARALLKNAPVVIL 505
Cdd:PRK11264 99 HrTVLENI-IEGPVIVKGEPKEEATA---------RARELLAKVGLAGKEtsyprrLSGGQQQRVAIARALAMRPEVILF 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1805558896 506 DEPTAALDIESELAVQKAIDNLVH-NRTVIIIAHRLSTIAGAGN-ILVIEEGQVVEQGTHAQLLSH 569
Cdd:PRK11264 169 DEPTSALDPELVGEVLNTIRQLAQeKRTMVIVTHEMSFARDVADrAIFMDQGRIVEQGPAKALFAD 234
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
354-568 |
6.14e-22 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 98.38 E-value: 6.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 354 EEGDGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLTPEQLNSLISVVFQDVWL-FD 432
Cdd:PRK09536 12 EFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsFE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 433 DTLLANIRIAR-PQATR---------QEVEEAARAAQCLEFISRlpqgwltPMGEmggqLSGGERQRISIARALLKNAPV 502
Cdd:PRK09536 92 FDVRQVVEMGRtPHRSRfdtwtetdrAAVERAMERTGVAQFADR-------PVTS----LSGGERQRVLLARALAQATPV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1805558896 503 VILDEPTAALDIESELAVQKAIDNLVHN-RTVIIIAHRLSTIAGAGNILVI-EEGQVVEQGTHAQLLS 568
Cdd:PRK09536 161 LLLDEPTASLDINHQVRTLELVRRLVDDgKTAVAAIHDLDLAARYCDELVLlADGRVRAAGPPADVLT 228
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
344-569 |
1.12e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 95.20 E-value: 1.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 344 IRFDNVSYRYEEG---DGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLTP----EQ 416
Cdd:PRK13649 3 INLQNVSYTYQAGtpfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKnkdiKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 417 LNSLISVVFQ--DVWLFDDTLLANIRIArPQ---ATRQEVEEAARAAQCL-----EFISRLPqgwltpmgemgGQLSGGE 486
Cdd:PRK13649 83 IRKKVGLVFQfpESQLFEETVLKDVAFG-PQnfgVSQEEAEALAREKLALvgiseSLFEKNP-----------FELSGGQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 487 RQRISIARALLKNAPVVILDEPTAALDIESELAVQKAIDNLVHN-RTVIIIAHRLSTIAG-AGNILVIEEGQVVEQGTHA 564
Cdd:PRK13649 151 MRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSgMTIVLVTHLMDDVANyADFVYVLEKGKLVLSGKPK 230
|
....*
gi 1805558896 565 QLLSH 569
Cdd:PRK13649 231 DIFQD 235
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
364-569 |
1.20e-21 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 96.71 E-value: 1.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 364 VSLTFPAASMSALVGASGAGKTTVTKL---LMRyadPQQGQISIGG---VDIRR---LTPEQLNslISVVFQDVWLFD-- 432
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAiagLER---PDSGRIRLGGevlQDSARgifLPPHRRR--IGYVFQEARLFPhl 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 433 ---DTLLANIRIARPQATRQEVEEAARAAQCLEFISRLPQgwltpmgemggQLSGGERQRISIARALLKNAPVVILDEPT 509
Cdd:COG4148 93 svrGNLLYGRKRAPRAERRISFDEVVELLGIGHLLDRRPA-----------TLSGGERQRVAIGRALLSSPRLLLMDEPL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1805558896 510 AALDIESELAVQKAIDNLvHNRT---VIIIAHRLSTIAG-AGNILVIEEGQVVEQGTHAQLLSH 569
Cdd:COG4148 162 AALDLARKAEILPYLERL-RDELdipILYVSHSLDEVARlADHVVLLEQGRVVASGPLAEVLSR 224
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
353-550 |
1.46e-21 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 93.63 E-value: 1.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 353 YEEGDGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLTPEQLNSLISVVFQDVWLFD 432
Cdd:PRK10247 15 YLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLFG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 433 DTLLANIrIARPQATRQEVEEAARAAQCLEFisRLPQGWLT-PMGEmggqLSGGERQRISIARALLKNAPVVILDEPTAA 511
Cdd:PRK10247 95 DTVYDNL-IFPWQIRNQQPDPAIFLDDLERF--ALPDTILTkNIAE----LSGGEKQRISLIRNLQFMPKVLLLDEITSA 167
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1805558896 512 LDIESELAVQKAIDNLV--HNRTVIIIAHRLSTIAGAGNIL 550
Cdd:PRK10247 168 LDESNKHNVNEIIHRYVreQNIAVLWVTHDKDEINHADKVI 208
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
344-513 |
1.76e-21 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 96.55 E-value: 1.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 344 IRFDNVSYRYeeGDGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLTPEQLNslISV 423
Cdd:PRK09452 15 VELRGISKSF--DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRH--VNT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 424 VFQDVWLFDD-TLLANIRIA-----RPQA-TRQEVEEAARAAQCLEFISRLPQgwltpmgemggQLSGGERQRISIARAL 496
Cdd:PRK09452 91 VFQSYALFPHmTVFENVAFGlrmqkTPAAeITPRVMEALRMVQLEEFAQRKPH-----------QLSGGQQQRVAIARAV 159
|
170
....*....|....*..
gi 1805558896 497 LKNAPVVILDEPTAALD 513
Cdd:PRK09452 160 VNKPKVLLLDESLSALD 176
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
344-561 |
1.77e-21 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 94.33 E-value: 1.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 344 IRFDNVSYRYeeGDGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYAD--PQQ---GQISIGGVDI--RRLTPEQ 416
Cdd:COG1117 12 IEVRNLNVYY--GDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPGArveGEILLDGEDIydPDVDVVE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 417 LNSLISVVFQ----------DvwlfddtllaNI----RIA--RPQATRQE-VEEAARAAQcL--EFISRLpqgwltpmGE 477
Cdd:COG1117 90 LRRRVGMVFQkpnpfpksiyD----------NVayglRLHgiKSKSELDEiVEESLRKAA-LwdEVKDRL--------KK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 478 MGGQLSGGERQRISIARAL-LKnaPVVIL-DEPTAALDIESELAVQKAIDNLVHNRTVIIIAH------RLSTiagagNI 549
Cdd:COG1117 151 SALGLSGGQQQRLCIARALaVE--PEVLLmDEPTSALDPISTAKIEELILELKKDYTIVIVTHnmqqaaRVSD-----YT 223
|
250
....*....|..
gi 1805558896 550 LVIEEGQVVEQG 561
Cdd:COG1117 224 AFFYLGELVEFG 235
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
361-555 |
2.20e-21 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 92.78 E-value: 2.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 361 LNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQI--SIGGVDIRRLTPEQLNSLISVVF--QDVWLFDDTLL 436
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwSNKNESEPSFEATRSRNRYSVAYaaQKPWLLNATVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 437 ANIRIARPqATRQEVEEAARAAQCLEFISRLPQGWLTPMGEMGGQLSGGERQRISIARALLKNAPVVILDEPTAALDIE- 515
Cdd:cd03290 97 ENITFGSP-FNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHl 175
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1805558896 516 SELAVQKAIDNLVHN--RTVIIIAHRLSTIAGAGNILVIEEG 555
Cdd:cd03290 176 SDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
361-568 |
2.31e-21 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 94.54 E-value: 2.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 361 LNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGvdirrltpeqlnsLISVVFQDVWLFDDTLLANIr 440
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-------------RISFSSQFSWIMPGTIKENI- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 441 IARPQATRQEVEEAARAAQCLEFISRLPQGWLTPMGEMGGQLSGGERQRISIARALLKNAPVVILDEPTAALDIESELAV 520
Cdd:cd03291 119 IFGVSYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEI 198
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1805558896 521 -QKAIDNLVHNRTVIIIAHRLSTIAGAGNILVIEEGQVVEQGTHAQLLS 568
Cdd:cd03291 199 fESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQS 247
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
376-569 |
2.41e-21 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 95.25 E-value: 2.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 376 LVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLTPEqlNSLISVVFQDVWLFDD-TLLANI----RIAR-PQATRQ 449
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPH--LRHINMVFQSYALFPHmTVEENVafglKMRKvPRAEIK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 450 E-VEEAARAAQCLEFISRLPQgwltpmgemggQLSGGERQRISIARALLKNAPVVILDEPTAALDIESELAVQKAIDNLV 528
Cdd:TIGR01187 79 PrVLEALRLVQLEEFADRKPH-----------QLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQ 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1805558896 529 HNR--TVIIIAHRLS-TIAGAGNILVIEEGQVVEQGTHAQLLSH 569
Cdd:TIGR01187 148 EQLgiTFVFVTHDQEeAMTMSDRIAIMRKGKIAQIGTPEEIYEE 191
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
268-576 |
2.61e-21 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 99.04 E-value: 2.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 268 VVVLS-GIVWVVTGTLN--LAFLIAAVAMIMRFaePMAMFISYTSVVELIASALQRIERFM-----AIAPLPVAEqsemP 339
Cdd:PLN03130 537 VTVVSfGVFTLLGGDLTpaRAFTSLSLFAVLRF--PLFMLPNLITQAVNANVSLKRLEELLlaeerVLLPNPPLE----P 610
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 340 ERYDIRFDNVSYRYE-EGDGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPqqgqISIGGVDIRrltpeqln 418
Cdd:PLN03130 611 GLPAISIKNGYFSWDsKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPP----RSDASVVIR-------- 678
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 419 SLISVVFQDVWLFDDTLLANIRIARP-QATRqeVEEAARAAQCLEFISRLPQGWLTPMGEMGGQLSGGERQRISIARALL 497
Cdd:PLN03130 679 GTVAYVPQVSWIFNATVRDNILFGSPfDPER--YERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVY 756
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 498 KNAPVVILDEPTAALDIESELAV-QKAIDNLVHNRTVIIIAHRLSTIAGAGNILVIEEGQVVEQGTHAQLLSHHGRYQAL 576
Cdd:PLN03130 757 SNSDVYIFDDPLSALDAHVGRQVfDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNGPLFQKL 836
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
344-562 |
3.80e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 93.61 E-value: 3.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 344 IRFDNVSYRYEEGDGH----ALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDirrlTPEQLN- 418
Cdd:PRK13633 5 IKCKNVSYKYESNEESteklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLD----TSDEENl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 419 ----SLISVVFQDVwlfDDTLLANI---RIA--------RPQATRQEVEEAARAAQCLEFISRLPQgwltpmgemggQLS 483
Cdd:PRK13633 81 wdirNKAGMVFQNP---DNQIVATIveeDVAfgpenlgiPPEEIRERVDESLKKVGMYEYRRHAPH-----------LLS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 484 GGERQRISIARALLKNAPVVILDEPTAALDIESELAVQKAIDNL--VHNRTVIIIAHRLSTIAGAGNILVIEEGQVVEQG 561
Cdd:PRK13633 147 GGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELnkKYGITIILITHYMEEAVEADRIIVMDSGKVVMEG 226
|
.
gi 1805558896 562 T 562
Cdd:PRK13633 227 T 227
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
359-579 |
5.57e-21 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 94.26 E-value: 5.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 359 HALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLTPEQLNSL---ISVVFQDVW------ 429
Cdd:PRK11308 29 KALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKLLrqkIQIVFQNPYgslnpr 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 430 -----LFDDTLLANIRIARPQATRQEVEEAARAAQCLEFISRLPQgwltpmgeMggqLSGGERQRISIARALLKNAPVVI 504
Cdd:PRK11308 109 kkvgqILEEPLLINTSLSAAERREKALAMMAKVGLRPEHYDRYPH--------M---FSGGQRQRIAIARALMLDPDVVV 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 505 LDEPTAALDIeselAVQKAIDNLV------HNRTVIIIAHRLSTIAG-AGNILVIEEGQVVEQGTHAQLLSH--HGRYQA 575
Cdd:PRK11308 178 ADEPVSALDV----SVQAQVLNLMmdlqqeLGLSYVFISHDLSVVEHiADEVMVMYLGRCVEKGTKEQIFNNprHPYTQA 253
|
....
gi 1805558896 576 LWQA 579
Cdd:PRK11308 254 LLSA 257
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
344-561 |
6.05e-21 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 91.12 E-value: 6.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 344 IRFDNVSYRYeeGDGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLTP--EQLNSLI 421
Cdd:cd03268 1 LKTNDLTKTY--GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEalRRIGALI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 422 svvfqDVWLFDDTLLA--NIRIARPQATRQEveeaARAAQCLEFISrlpqgwltpMGEMG----GQLSGGERQRISIARA 495
Cdd:cd03268 79 -----EAPGFYPNLTAreNLRLLARLLGIRK----KRIDEVLDVVG---------LKDSAkkkvKGFSLGMKQRLGIALA 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1805558896 496 LLKNAPVVILDEPTAALDIESELAVQKAIDNLV-HNRTVIIIAHRLSTIAG-AGNILVIEEGQVVEQG 561
Cdd:cd03268 141 LLGNPDLLILDEPTNGLDPDGIKELRELILSLRdQGITVLISSHLLSEIQKvADRIGIINKGKLIEEG 208
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
34-321 |
6.34e-21 |
|
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family represents a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in this family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349983 [Multi-domain] Cd Length: 292 Bit Score: 93.38 E-value: 6.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 34 MLALLLAAFMQGIAFACLYPIIDALLRGDAPQLLNWAMAFSVAAIVTLVLRWYGLGFEYRGHlAQATHELRLRLGEQLRR 113
Cdd:cd07346 6 LLLLLATALGLALPLLTKLLIDDVIPAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLG-QRVVFDLRRDLFRHLQR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 114 VPLEKLQRGRAGEMNALLLGSVDENLNYVIAIANILLLTIVTPLTASLATLWIDWRLGLVMLLIFPLLVPFYYWRRPAMR 193
Cdd:cd07346 85 LSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFRRRIR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 194 RQMQTLGEAHQRLSGDIVEFAQGMMVLRTCGSDADKSRALLAHFNALENLQTRTHRQGAGATMLIASVVELGLQVVVLSG 273
Cdd:cd07346 165 KASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTALVLLYG 244
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1805558896 274 IVWVVTGTLNLAFLIAAVAMIMRFAEPMAMFISYTSVVELIASALQRI 321
Cdd:cd07346 245 GYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
360-561 |
7.17e-21 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 92.01 E-value: 7.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 360 ALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLTPEQLnSLISVVF---QDVWlFD---- 432
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFL-RRIGVVFgqkTQLW-WDlpvi 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 433 DTLLANIRIAR--PQATRQEVEEAARAAQCLEFISrlpqgwlTPMGemggQLSGGERQRISIARALLKNAPVVILDEPTA 510
Cdd:cd03267 114 DSFYLLAAIYDlpPARFKKRLDELSELLDLEELLD-------TPVR----QLSLGQRMRAEIAAALLHEPEILFLDEPTI 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1805558896 511 ALDIESELAVQKAIDNLVHNR--TVIIIAHRLSTIAG-AGNILVIEEGQVVEQG 561
Cdd:cd03267 183 GLDVVAQENIRNFLKEYNRERgtTVLLTSHYMKDIEAlARRVLVIDKGRLLYDG 236
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
348-558 |
1.16e-20 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 96.33 E-value: 1.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 348 NVSYRYEEGDGH--ALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLTPEQLNSL----I 421
Cdd:PRK10535 9 DIRRSYPSGEEQveVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQLrrehF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 422 SVVFQDVWLFDD-TLLANIRIArpqATRQEVEEAARAAQCLEFISRLpqGWLTPMGEMGGQLSGGERQRISIARALLKNA 500
Cdd:PRK10535 89 GFIFQRYHLLSHlTAAQNVEVP---AVYAGLERKQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQQRVSIARALMNGG 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1805558896 501 PVVILDEPTAALDIESELAVQKAIDNLV-HNRTVIIIAHRLSTIAGAGNILVIEEGQVV 558
Cdd:PRK10535 164 QVILADEPTGALDSHSGEEVMAILHQLRdRGHTVIIVTHDPQVAAQAERVIEIRDGEIV 222
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
344-561 |
1.73e-20 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 90.12 E-value: 1.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 344 IRFDNVSYRYE--EGDGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRlTPEQLNSLI 421
Cdd:cd03266 2 ITADALTKRFRdvKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 422 SVVFQDVWLFDD-TLLANIRI------ARPQATRQEVEEAARAAQCLEFISRlpqgwltpmgeMGGQLSGGERQRISIAR 494
Cdd:cd03266 81 GFVSDSTGLYDRlTARENLEYfaglygLKGDELTARLEELADRLGMEELLDR-----------RVGGFSTGMRQKVAIAR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1805558896 495 ALLKNAPVVILDEPTAALDIeseLAVQKAIDNLVHNR----TVIIIAHRLSTIAG-AGNILVIEEGQVVEQG 561
Cdd:cd03266 150 ALVHDPPVLLLDEPTTGLDV---MATRALREFIRQLRalgkCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
344-569 |
2.31e-20 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 90.54 E-value: 2.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 344 IRFDNVSYRYeeGDGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRrlTPEQLNSLI-- 421
Cdd:PRK09493 2 IEFKNVSKHF--GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVN--DPKVDERLIrq 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 422 --SVVFQDVWLFDD-TLLANIRIArPQATRQEVEEAARAaQCLEFISRLpqGWLTPMGEMGGQLSGGERQRISIARALLK 498
Cdd:PRK09493 78 eaGMVFQQFYLFPHlTALENVMFG-PLRVRGASKEEAEK-QARELLAKV--GLAERAHHYPSELSGGQQQRVAIARALAV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1805558896 499 NAPVVILDEPTAALDIESELAVQKAIDNLVHN-RTVIIIAHRLSTIAGAGNILV-IEEGQVVEQGTHAQLLSH 569
Cdd:PRK09493 154 KPKLMLFDEPTSALDPELRHEVLKVMQDLAEEgMTMVIVTHEIGFAEKVASRLIfIDKGRIAEDGDPQVLIKN 226
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
342-555 |
2.61e-20 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 91.00 E-value: 2.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 342 YDIRFDNVSYRYeeGDGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYAD-----PQQGQISIGGVDI--RRLTP 414
Cdd:PRK14243 9 TVLRTENLNVYY--GSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDlipgfRVEGKVTFHGKNLyaPDVDP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 415 EQLNSLISVVFQDVWLFDDTLLANI----RIARPQATRQEVEEAA--RAAQCLEFISRLPQGwltpmgemGGQLSGGERQ 488
Cdd:PRK14243 87 VEVRRRIGMVFQKPNPFPKSIYDNIaygaRINGYKGDMDELVERSlrQAALWDEVKDKLKQS--------GLSLSGGQQQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1805558896 489 RISIARALLKNAPVVILDEPTAALDIESELAVQKAIDNLVHNRTVIIIAH------RLSTIAGAGNILVIEEG 555
Cdd:PRK14243 159 RLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHnmqqaaRVSDMTAFFNVELTEGG 231
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
251-566 |
3.89e-20 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 95.23 E-value: 3.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 251 GAGATMLIASVVELGLQVVVLSgIVWVVTGTLN-LAFLIAAVAMIMRFAEPMAMFISYT---SVVELIASALQRIERFMA 326
Cdd:PTZ00243 1203 GVIGTMLRATSQEIGLVSLSLT-MAMQTTATLNwLVRQVATVEADMNSVERLLYYTDEVpheDMPELDEEVDALERRTGM 1281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 327 IAPL-------PVAEQSEMPERYD---IRFDNVSYRYEEGDGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYAD 396
Cdd:PTZ00243 1282 AADVtgtvviePASPTSAAPHPVQagsLVFEGVQMRYREGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVE 1361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 397 PQQGQISIGGVDIRRLTPEQLNSLISVVFQDVWLFDDTLLANIRiarP--QATRQEVEEAARAAQCLEFISRLPQGWLTP 474
Cdd:PTZ00243 1362 VCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNVD---PflEASSAEVWAALELVGLRERVASESEGIDSR 1438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 475 MGEMGGQLSGGERQRISIARALLKNAPVVIL-DEPTAALDIESELAVQKAIDNLVHNRTVIIIAHRLSTIAGAGNILVIE 553
Cdd:PTZ00243 1439 VLEGGSNYSVGQRQLMCMARALLKKGSGFILmDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMD 1518
|
330
....*....|...
gi 1805558896 554 EGQVVEQGTHAQL 566
Cdd:PTZ00243 1519 HGAVAEMGSPREL 1531
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
356-561 |
4.13e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 89.97 E-value: 4.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 356 GDGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMR----YADPQ-QGQISIGGVDIRRLTPEQLNSLISVVFQ---- 426
Cdd:PRK14247 14 GQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRlielYPEARvSGEVYLDGQDIFKMDVIELRRRVQMVFQipnp 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 427 --DVWLFDDTLLAnIRIARPQATRQEVEEaaRAAQCLEfISRLPQGWLTPMGEMGGQLSGGERQRISIARALLKNAPVVI 504
Cdd:PRK14247 94 ipNLSIFENVALG-LKLNRLVKSKKELQE--RVRWALE-KAQLWDEVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1805558896 505 LDEPTAALDIESELAVQKAIDNLVHNRTVIIIAHRLSTIAGAGN-ILVIEEGQVVEQG 561
Cdd:PRK14247 170 ADEPTANLDPENTAKIESLFLELKKDMTIVLVTHFPQQAARISDyVAFLYKGQIVEWG 227
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
344-558 |
4.80e-20 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 89.16 E-value: 4.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 344 IRFDNVSYRYEeGDGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLTPEQ---LNSL 420
Cdd:PRK10908 2 IRFEHVSKAYL-GGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 421 ISVVFQDV-WLFDDTLLANIRIARPQATRQEVEEAARAAQCLEFISRLPQGWLTPMgemggQLSGGERQRISIARALLKN 499
Cdd:PRK10908 81 IGMIFQDHhLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPI-----QLSGGEQQRVGIARAVVNK 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1805558896 500 APVVILDEPTAALDIESELAVQKAIDNLvhNR---TVIIIAHRLSTIAGAG-NILVIEEGQVV 558
Cdd:PRK10908 156 PAVLLADEPTGNLDDALSEGILRLFEEF--NRvgvTVLMATHDIGLISRRSyRMLTLSDGHLH 216
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
348-569 |
4.85e-20 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 93.60 E-value: 4.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 348 NVSYRYEEGDGHALNHVSLTFPAASMSALVGASGAGKT----TVTKLLMRYADPQQGQISIGGVDIRRLTPEQLNSL--- 420
Cdd:COG4172 13 SVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELRRIrgn 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 421 -ISVVFQD-------VWLFDDTLLANIRIARPqATRQEVEeaARAAQCLEFIsRLPQgwltPMGEMGG---QLSGGERQR 489
Cdd:COG4172 93 rIAMIFQEpmtslnpLHTIGKQIAEVLRLHRG-LSGAAAR--ARALELLERV-GIPD----PERRLDAyphQLSGGQRQR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 490 ISIARALLkNAP-VVILDEPTAALDIeselAVQKAIDNLV------HNRTVIIIAHRLSTIAG-AGNILVIEEGQVVEQG 561
Cdd:COG4172 165 VMIAMALA-NEPdLLIADEPTTALDV----TVQAQILDLLkdlqreLGMALLLITHDLGVVRRfADRVAVMRQGEIVEQG 239
|
....*...
gi 1805558896 562 THAQLLSH 569
Cdd:COG4172 240 PTAELFAA 247
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
336-562 |
5.40e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 91.07 E-value: 5.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 336 SEMPERYDI--RFDNVSYRYEEGDGH---ALNHVSLTFPAASMSALVGASGAGKTTVTK-----LLMRYADPQQGQISIG 405
Cdd:PRK13631 12 VPNPLSDDIilRVKNLYCVFDEKQENelvALNNISYTFEKNKIYFIIGNSGSGKSTLVThfnglIKSKYGTIQVGDIYIG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 406 G-VDIRRLTP----------EQLNSLISVVFQ--DVWLFDDTLLANIRIArPQATRQEVEEAA-RAAQCLE-------FI 464
Cdd:PRK13631 92 DkKNNHELITnpyskkiknfKELRRRVSMVFQfpEYQLFKDTIEKDIMFG-PVALGVKKSEAKkLAKFYLNkmglddsYL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 465 SRLPQGwltpmgemggqLSGGERQRISIARALLKNAPVVILDEPTAALDIESELAVQKAI-DNLVHNRTVIIIAHRLSTI 543
Cdd:PRK13631 171 ERSPFG-----------LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLIlDAKANNKTVFVITHTMEHV 239
|
250 260
....*....|....*....|
gi 1805558896 544 AGAGN-ILVIEEGQVVEQGT 562
Cdd:PRK13631 240 LEVADeVIVMDKGKILKTGT 259
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
344-565 |
5.81e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 90.49 E-value: 5.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 344 IRFDNVSYRYEEG---DGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDI--RRLTPEQLN 418
Cdd:PRK13637 3 IKIENLTHIYMEGtpfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 419 SLISVVFQ--DVWLFDDTLLANIRIArPQ---ATRQEVEEAARAAQCLEFISRLPQGWLTPMgemggQLSGGERQRISIA 493
Cdd:PRK13637 83 KKVGLVFQypEYQLFEETIEKDIAFG-PInlgLSEEEIENRVKRAMNIVGLDYEDYKDKSPF-----ELSGGQKRRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1805558896 494 RALLKNAPVVILDEPTAALDIESELAVQKAIDNL--VHNRTVIIIAHRLSTIAG-AGNILVIEEGQVVEQGTHAQ 565
Cdd:PRK13637 157 GVVAMEPKILILDEPTAGLDPKGRDEILNKIKELhkEYNMTIILVSHSMEDVAKlADRIIVMNKGKCELQGTPRE 231
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
360-566 |
1.10e-19 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 88.89 E-value: 1.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 360 ALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLtPEQLNSLISVV--FQDVWLFDD-TLL 436
Cdd:PRK11300 20 AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGL-PGHQIARMGVVrtFQHVRLFREmTVI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 437 ANIRIAR---------------PQATRQEVEEAARAAQCLEFISrlpqgwLTPMG-EMGGQLSGGERQRISIARALLKNA 500
Cdd:PRK11300 99 ENLLVAQhqqlktglfsgllktPAFRRAESEALDRAATWLERVG------LLEHAnRQAGNLAYGQQRRLEIARCMVTQP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1805558896 501 PVVILDEPTAALDIESELAVQKAIDNL--VHNRTVIIIAHRLSTIAGAGN-ILVIEEGQVVEQGTHAQL 566
Cdd:PRK11300 173 EILMLDEPAAGLNPKETKELDELIAELrnEHNVTVLLIEHDMKLVMGISDrIYVVNQGTPLANGTPEEI 241
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
344-562 |
1.49e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 89.12 E-value: 1.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 344 IRFDNVSYRYEEG---DGHALNHVSLTFPAASMSALVGASGAGKTTvtklLMRYAD----PQQGQISIGGVDIrrlTPE- 415
Cdd:PRK13641 3 IKFENVDYIYSPGtpmEKKGLDNISFELEEGSFVALVGHTGSGKST----LMQHFNallkPSSGTITIAGYHI---TPEt 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 416 ------QLNSLISVVFQ--DVWLFDDTLLANIRIArPQ---ATRQEVEEAAraaqcLEFISRLpqGWLTPMGEMGG-QLS 483
Cdd:PRK13641 76 gnknlkKLRKKVSLVFQfpEAQLFENTVLKDVEFG-PKnfgFSEDEAKEKA-----LKWLKKV--GLSEDLISKSPfELS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 484 GGERQRISIARALLKNAPVVILDEPTAALDIESELAV-QKAIDNLVHNRTVIIIAHRLSTIAG-AGNILVIEEGQVVEQG 561
Cdd:PRK13641 148 GGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMmQLFKDYQKAGHTVILVTHNMDDVAEyADDVLVLEHGKLIKHA 227
|
.
gi 1805558896 562 T 562
Cdd:PRK13641 228 S 228
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
344-569 |
1.50e-19 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 87.98 E-value: 1.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 344 IRFDNVSYRYeeGDGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLTPEQLNSL-IS 422
Cdd:cd03218 1 LRAENLSKRY--GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLgIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 423 VVFQDVWLFDD-TLLANIRIARPQATRQEVEEAARAAQCL-EF-ISRLPQgwltpmgEMGGQLSGGERQRISIARALLKN 499
Cdd:cd03218 79 YLPQEASIFRKlTVEENILAVLEIRGLSKKEREEKLEELLeEFhITHLRK-------SKASSLSGGERRRVEIARALATN 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 500 APVVILDEPTAALDIESELAVQKAIDNLV----------HN-RTVIIIAHRlstiagagnILVIEEGQVVEQGTHAQLLS 568
Cdd:cd03218 152 PKFLLLDEPFAGVDPIAVQDIQKIIKILKdrgigvlitdHNvRETLSITDR---------AYIIYEGKVLAEGTPEEIAA 222
|
.
gi 1805558896 569 H 569
Cdd:cd03218 223 N 223
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
344-559 |
2.00e-19 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 87.49 E-value: 2.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 344 IRFDNVSYRYEEGDG--HALNHVSLTFPAASMSALVGASGAGKTTvtkLLMRYA---DPQQGQISIGGVDIRRLTPEQL- 417
Cdd:COG4181 9 IELRGLTKTVGTGAGelTILKGISLEVEAGESVAIVGASGSGKST---LLGLLAgldRPTSGTVRLAGQDLFALDEDARa 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 418 ---NSLISVVFQDVWLFDD-TLLANIriARPQATRQEVEEAARAAQCLEfisrlpqgwltpmgEMG---------GQLSG 484
Cdd:COG4181 86 rlrARHVGFVFQSFQLLPTlTALENV--MLPLELAGRRDARARARALLE--------------RVGlghrldhypAQLSG 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1805558896 485 GERQRISIARALLKNAPVVILDEPTAALDIESELAVQKAIDNLvhNR----TVIIIAHRLSTIAGAGNILVIEEGQVVE 559
Cdd:COG4181 150 GEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFEL--NRergtTLVLVTHDPALAARCDRVLRLRAGRLVE 226
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
343-569 |
2.32e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 88.91 E-value: 2.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 343 DIRFDNVSYRYEEG---DGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGG----VDIRRLTP- 414
Cdd:PRK13645 6 DIILDNVSYTYAKKtpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaipANLKKIKEv 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 415 EQLNSLISVVFQ--DVWLFDDTLLANIRIARPQATRQEVEEAARAAQCLEFISrLPQGWL--TPMgemggQLSGGERQRI 490
Cdd:PRK13645 86 KRLRKEIGLVFQfpEYQLFQETIEKDIAFGPVNLGENKQEAYKKVPELLKLVQ-LPEDYVkrSPF-----ELSGGQKRRV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 491 SIARALLKNAPVVILDEPTAALDIESELAVQKAIDNLVHN--RTVIIIAHRLSTIAG-AGNILVIEEGQVVEQGTHAQLL 567
Cdd:PRK13645 160 ALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEykKRIIMVTHNMDQVLRiADEVIVMHEGKVISIGSPFEIF 239
|
..
gi 1805558896 568 SH 569
Cdd:PRK13645 240 SN 241
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
344-576 |
2.87e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 88.25 E-value: 2.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 344 IRFDNVSYRY-EEGDGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGvdiRRLTPE---QLNS 419
Cdd:PRK13650 5 IEVKNLTFKYkEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDG---DLLTEEnvwDIRH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 420 LISVVFQD-------VWLFDDTL--LANIRIARpQATRQEVEEAARAAQCLEFISRLPqgwltpmgemgGQLSGGERQRI 490
Cdd:PRK13650 82 KIGMVFQNpdnqfvgATVEDDVAfgLENKGIPH-EEMKERVNEALELVGMQDFKEREP-----------ARLSGGQKQRV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 491 SIARALLKNAPVVILDEPTAALDIESELAVQKAIDNLV--HNRTVIIIAHRLSTIAGAGNILVIEEGQVVEQGTHAQLLS 568
Cdd:PRK13650 150 AIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRddYQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFS 229
|
....*...
gi 1805558896 569 HHGRYQAL 576
Cdd:PRK13650 230 RGNDLLQL 237
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
348-568 |
3.28e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 87.94 E-value: 3.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 348 NVSYRYEeGDGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLTPEQLNSLISVVFQ- 426
Cdd:PRK13652 8 DLCYSYS-GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQn 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 427 -DVWLFDDTLLANIRIA------RPQATRQEVEEAARAAQCLEFISRLPQgwltpmgemggQLSGGERQRISIARALLKN 499
Cdd:PRK13652 87 pDDQIFSPTVEQDIAFGpinlglDEETVAHRVSSALHMLGLEELRDRVPH-----------HLSGGEKKRVAIAGVIAME 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1805558896 500 APVVILDEPTAALDIESELAVQKAIDNLV--HNRTVIIIAHRLSTIAG-AGNILVIEEGQVVEQGTHAQLLS 568
Cdd:PRK13652 156 PQVLVLDEPTAGLDPQGVKELIDFLNDLPetYGMTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEEIFL 227
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
355-537 |
3.35e-19 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 85.94 E-value: 3.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 355 EGDGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGG--VDIRRLTPEQLNSLISVVFQDVwlfD 432
Cdd:TIGR01166 2 PGGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGepLDYSRKGLLERRQRVGLVFQDP---D 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 433 DTLLA------------NIRIARPQATRQeVEEAARAAQCLEFISRLPQgwltpmgemggQLSGGERQRISIARALLKNA 500
Cdd:TIGR01166 79 DQLFAadvdqdvafgplNLGLSEAEVERR-VREALTAVGASGLRERPTH-----------CLSGGEKKRVAIAGAVAMRP 146
|
170 180 190
....*....|....*....|....*....|....*..
gi 1805558896 501 PVVILDEPTAALDIESELAVQKAIDNLVHNRTVIIIA 537
Cdd:TIGR01166 147 DVLLLDEPTAGLDPAGREQMLAILRRLRAEGMTVVIS 183
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
345-567 |
3.71e-19 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 87.54 E-value: 3.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 345 RFDNVSYRYEegdGHALNH-VSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLTPEQLNSLISV 423
Cdd:PRK10575 13 ALRNVSFRVP---GRTLLHpLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 424 VFQDVWLFDD-TLLANIRIAR----------PQATRQEVEEAARAAQCLEFISRLPQgwltpmgemggQLSGGERQRISI 492
Cdd:PRK10575 90 LPQQLPAAEGmTVRELVAIGRypwhgalgrfGAADREKVEEAISLVGLKPLAHRLVD-----------SLSGGERQRAWI 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1805558896 493 ARALLKNAPVVILDEPTAALDIESELAVQKAIDNLVHNR--TVIIIAHRLSTIAGAGNILV-IEEGQVVEQGTHAQLL 567
Cdd:PRK10575 159 AMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERglTVIAVLHDINMAARYCDYLVaLRGGEMIAQGTPAELM 236
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
356-569 |
4.27e-19 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 90.92 E-value: 4.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 356 GDGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYAdPQQGQISIGGVDIRRLTPEQL---NSLISVVFQDVW--- 429
Cdd:PRK15134 297 DHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNLNRRQLlpvRHRIQVVFQDPNssl 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 430 ---LFDDTLLAN-IRIARPQATRQEVEEAARAAqclefisrlpqgwltpMGEMG----------GQLSGGERQRISIARA 495
Cdd:PRK15134 376 nprLNVLQIIEEgLRVHQPTLSAAQREQQVIAV----------------MEEVGldpetrhrypAEFSGGQRQRIAIARA 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 496 LLKNAPVVILDEPTAALDieseLAVQKAIDNLV------HNRTVIIIAHRLSTI-AGAGNILVIEEGQVVEQGTHAQLLS 568
Cdd:PRK15134 440 LILKPSLIILDEPTSSLD----KTVQAQILALLkslqqkHQLAYLFISHDLHVVrALCHQVIVLRQGEVVEQGDCERVFA 515
|
.
gi 1805558896 569 H 569
Cdd:PRK15134 516 A 516
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
340-562 |
4.45e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 87.60 E-value: 4.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 340 ERYDIRFDNVSYRYEEGDgHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGG--VDIRRLTPEQL 417
Cdd:PRK13636 2 EDYILKVEELNYNYSDGT-HALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpIDYSRKGLMKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 418 NSLISVVFQD-------VWLFDDTLLANIRIARPQATRQEVEEAARAAQCLEFISRLPQGWLtpmgemggqlSGGERQRI 490
Cdd:PRK13636 81 RESVGMVFQDpdnqlfsASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCL----------SFGQKKRV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 491 SIARALLKNAPVVILDEPTAALD-------IESELAVQKAIDnlvhnRTVIIIAHRLSTIA-GAGNILVIEEGQVVEQGT 562
Cdd:PRK13636 151 AIAGVLVMEPKVLVLDEPTAGLDpmgvseiMKLLVEMQKELG-----LTIIIATHDIDIVPlYCDNVFVMKEGRVILQGN 225
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
361-538 |
4.95e-19 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 86.17 E-value: 4.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 361 LNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQ---QGQISIGGvdiRRLTPEQLNSLISVVFQDvwlfdDTLL- 436
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNG---QPRKPDQFQKCVAYVRQD-----DILLp 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 437 -----------ANIRIARPQATRQEVEEAAraaqclefISRLPQGWLTPMGEMG-GQLSGGERQRISIARALLKNAPVVI 504
Cdd:cd03234 95 gltvretltytAILRLPRKSSDAIRKKRVE--------DVLLRDLALTRIGGNLvKGISGGERRRVSIAVQLLWDPKVLI 166
|
170 180 190
....*....|....*....|....*....|....*
gi 1805558896 505 LDEPTAALDIESELAVQKAIDNLVH-NRTVIIIAH 538
Cdd:cd03234 167 LDEPTSGLDSFTALNLVSTLSQLARrNRIVILTIH 201
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
237-568 |
6.26e-19 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 91.51 E-value: 6.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 237 FNALENLQTRTHRQGAGATMLIasvveLGLQVVVLSGIVWVVTGTLNLAFLIAAVAMIMRF-------AEPMAMFISYTS 309
Cdd:TIGR01271 1123 FIAVTFIAIGTNQDGEGEVGII-----LTLAMNILSTLQWAVNSSIDVDGLMRSVSRVFKFidlpqeePRPSGGGGKYQL 1197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 310 VVELIasalqrIERFMAiaplpvaeQSEMPERYDIRFDNVSYRYEEGDGHALNHVSLTFPAASMSALVGASGAGKTTVTK 389
Cdd:TIGR01271 1198 STVLV------IENPHA--------QKCWPSGGQMDVQGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLS 1263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 390 LLMRYADpQQGQISIGGVDIRRLTPEQLNSLISVVFQDVWLFDDTLLANIRiARPQATRQEVEEAARAAQCLEFISRLPQ 469
Cdd:TIGR01271 1264 ALLRLLS-TEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLD-PYEQWSDEEIWKVAEEVGLKSVIEQFPD 1341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 470 GWLTPMGEMGGQLSGGERQRISIARALLKNAPVVILDEPTAALDIESELAVQKAIDNLVHNRTVIIIAHRLSTIAGAGNI 549
Cdd:TIGR01271 1342 KLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQF 1421
|
330
....*....|....*....
gi 1805558896 550 LVIEEGQVVEQGTHAQLLS 568
Cdd:TIGR01271 1422 LVIEGSSVKQYDSIQKLLN 1440
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
361-566 |
6.43e-19 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 91.51 E-value: 6.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 361 LNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGvdirrltpeqlnsLISVVFQDVWLFDDTLLANIr 440
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-------------RISFSPQTSWIMPGTIKDNI- 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 441 IARPQATRQEVEEAARAAQCLEFISRLPQGWLTPMGEMGGQLSGGERQRISIARALLKNAPVVILDEPTAALDIESELAV 520
Cdd:TIGR01271 508 IFGLSYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEI 587
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1805558896 521 -QKAIDNLVHNRTVIIIAHRLSTIAGAGNILVIEEGQVVEQGTHAQL 566
Cdd:TIGR01271 588 fESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSEL 634
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
360-579 |
6.73e-19 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 88.22 E-value: 6.73e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 360 ALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLTPEQL---NSLISVVFQDV-------W 429
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWravRSDIQMIFQDPlaslnprM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 430 LFDDTLLANIRIARPQATRQEVEEAARAAQCL-----EFISRLPQgwltpmgemggQLSGGERQRISIARALLKNAPVVI 504
Cdd:PRK15079 116 TIGEIIAEPLRTYHPKLSRQEVKDRVKAMMLKvgllpNLINRYPH-----------EFSGGQCQRIGIARALILEPKLII 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 505 LDEPTAALDIeselAVQKAIDNLVHN------RTVIIIAHRLSTIAGAGN-ILVIEEGQVVEQGTHAQLLSH--HGRYQA 575
Cdd:PRK15079 185 CDEPVSALDV----SIQAQVVNLLQQlqremgLSLIFIAHDLAVVKHISDrVLVMYLGHAVELGTYDEVYHNplHPYTKA 260
|
....
gi 1805558896 576 LWQA 579
Cdd:PRK15079 261 LMSA 264
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
348-566 |
7.25e-19 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 86.04 E-value: 7.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 348 NVSYryeeGDGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLTPEQLNSL-ISVVFQ 426
Cdd:TIGR03410 7 NVYY----GQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERARAgIAYVPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 427 DVWLFDD-TLLANIRI---ARPQATRQEVEEA-ARAAQCLEFISRlpqgwltpmgeMGGQLSGGERQRISIARALLKNAP 501
Cdd:TIGR03410 83 GREIFPRlTVEENLLTglaALPRRSRKIPDEIyELFPVLKEMLGR-----------RGGDLSGGQQQQLAIARALVTRPK 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1805558896 502 VVILDEPTAAL------DIEselavqKAIDNLVHNR--TVIIIAHRLS-TIAGAGNILVIEEGQVVEQGTHAQL 566
Cdd:TIGR03410 152 LLLLDEPTEGIqpsiikDIG------RVIRRLRAEGgmAILLVEQYLDfARELADRYYVMERGRVVASGAGDEL 219
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
347-584 |
7.75e-19 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 86.66 E-value: 7.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 347 DNVSYRYEEGD---GHA----LNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLTPEQLNS 419
Cdd:PRK10419 7 SGLSHHYAHGGlsgKHQhqtvLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 420 L---ISVVFQDV-----------WLFDDTL--LANIRIARPQATRQEVEEAARAAqcLEFISRLPQgwltpmgemggQLS 483
Cdd:PRK10419 87 FrrdIQMVFQDSisavnprktvrEIIREPLrhLLSLDKAERLARASEMLRAVDLD--DSVLDKRPP-----------QLS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 484 GGERQRISIARALLKNAPVVILDEPTAALDIESELAVQKAIDNLVHNRTV--IIIAHRLSTIAG-AGNILVIEEGQVVEQ 560
Cdd:PRK10419 154 GGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTacLFITHDLRLVERfCQRVMVMDNGQIVET 233
|
250 260
....*....|....*....|....*
gi 1805558896 561 GTHAQLLS-HHGRYQALWQAQMAAR 584
Cdd:PRK10419 234 QPVGDKLTfSSPAGRVLQNAVLPAF 258
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
344-559 |
7.95e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 89.74 E-value: 7.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 344 IRFDNVSYRYeeGDGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIG-GVDI-----RRltpEQL 417
Cdd:COG0488 316 LELEGLSKSY--GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGeTVKIgyfdqHQ---EEL 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 418 NSlisvvfqdvwlfDDTLLANIRIARPQATRQEVeeaaRAaqcleFISRL---PQGWLTPMGEmggqLSGGERQRISIAR 494
Cdd:COG0488 391 DP------------DKTVLDELRDGAPGGTEQEV----RG-----YLGRFlfsGDDAFKPVGV----LSGGEKARLALAK 445
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1805558896 495 ALLKNAPVVILDEPTAALDIESELAVQKAIDNlvHNRTVIIIAH-R--LSTIagAGNILVIEEGQVVE 559
Cdd:COG0488 446 LLLSPPNVLLLDEPTNHLDIETLEALEEALDD--FPGTVLLVSHdRyfLDRV--ATRILEFEDGGVRE 509
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
365-569 |
8.69e-19 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 88.94 E-value: 8.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 365 SLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLTPEQLNSL----ISVVFQDVWL------FDDT 434
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVrrkkIAMVFQSFALmphmtvLDNT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 435 LLANIRIARPQATRQE-VEEAARAAQCLEFISRLPQgwltpmgemggQLSGGERQRISIARALLKNAPVVILDEPTAALD 513
Cdd:PRK10070 128 AFGMELAGINAEERREkALDALRQVGLENYAHSYPD-----------ELSGGMRQRVGLARALAINPDILLMDEAFSALD 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1805558896 514 --IESELAVQKAIDNLVHNRTVIIIAHRLSTIAGAGN-ILVIEEGQVVEQGTHAQLLSH 569
Cdd:PRK10070 197 plIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDrIAIMQNGEVVQVGTPDEILNN 255
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
344-513 |
1.02e-18 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 86.07 E-value: 1.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 344 IRFDNVSYRYEEGDG--HALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLTPEQlnsli 421
Cdd:COG4525 4 LTVRHVSVRYPGGGQpqPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADR----- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 422 SVVFQD----VWLfddTLLANI----RIARpqatrqeVEEAARAAQCLEFISrlpqgwLTPMGEMGG----QLSGGERQR 489
Cdd:COG4525 79 GVVFQKdallPWL---NVLDNVafglRLRG-------VPKAERRARAEELLA------LVGLADFARrriwQLSGGMRQR 142
|
170 180
....*....|....*....|....
gi 1805558896 490 ISIARALLKNAPVVILDEPTAALD 513
Cdd:COG4525 143 VGIARALAADPRFLLMDEPFGALD 166
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
344-568 |
1.37e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 86.30 E-value: 1.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 344 IRFDNVSYRYE-EGDGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGvdiRRLTPEQLNSL-- 420
Cdd:PRK13642 5 LEVENLVFKYEkESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDG---ELLTAENVWNLrr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 421 -ISVVFQD-------VWLFDDTL--LANIRIARPQATRQeVEEAARAAQCLEFISRLPqgwltpmgemgGQLSGGERQRI 490
Cdd:PRK13642 82 kIGMVFQNpdnqfvgATVEDDVAfgMENQGIPREEMIKR-VDEALLAVNMLDFKTREP-----------ARLSGGQKQRV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 491 SIARALLKNAPVVILDEPTAALDIESELAVQKAIDNL--VHNRTVIIIAHRLSTIAGAGNILVIEEGQVVEQGTHAQLLS 568
Cdd:PRK13642 150 AVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIkeKYQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFA 229
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
302-538 |
1.51e-18 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 89.09 E-value: 1.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 302 AMFISYTSVVElIASALQRIERFMAIAPLPVAEQSEMPERYDIRFDNVSYRY---EEGDGHALNHVSLTFPAASMSALVG 378
Cdd:TIGR03269 239 AIWLENGEIKE-EGTPDEVVAVFMEGVSEVEKECEVEVGEPIIKVRNVSKRYisvDRGVVKAVDNVSLEVKEGEIFGIVG 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 379 ASGAGKTTVTKLLMRYADPQQGQIS--IGG--VDIRRLTPE---QLNSLISVVFQDVWLFD-----DTLLANIRIARPQ- 445
Cdd:TIGR03269 318 TSGAGKTTLSKIIAGVLEPTSGEVNvrVGDewVDMTKPGPDgrgRAKRYIGILHQEYDLYPhrtvlDNLTEAIGLELPDe 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 446 -ATRQEV---------EEAARaaqclEFISRLPQgwltpmgemggQLSGGERQRISIARALLKNAPVVILDEPTAALDIE 515
Cdd:TIGR03269 398 lARMKAVitlkmvgfdEEKAE-----EILDKYPD-----------ELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPI 461
|
250 260
....*....|....*....|....*
gi 1805558896 516 SELAVQKAIDNLVH--NRTVIIIAH 538
Cdd:TIGR03269 462 TKVDVTHSILKAREemEQTFIIVSH 486
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
268-576 |
1.77e-18 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 90.04 E-value: 1.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 268 VVVLSGIVWVVTG---TLNLAFLIAAVAMIMRFaePMAMFISYTSVVELIASALQRIERFM-----AIAPLPVAEqsemP 339
Cdd:PLN03232 537 VTLVSFGVFVLLGgdlTPARAFTSLSLFAVLRS--PLNMLPNLLSQVVNANVSLQRIEELLlseerILAQNPPLQ----P 610
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 340 ERYDIRFDNVSYRYE-EGDGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQgqisIGGVDIRrltpeqln 418
Cdd:PLN03232 611 GAPAISIKNGYFSWDsKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAE----TSSVVIR-------- 678
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 419 SLISVVFQDVWLFDDTLLANIRIArpqaTRQEVEEAARA--AQCLEF-ISRLPQGWLTPMGEMGGQLSGGERQRISIARA 495
Cdd:PLN03232 679 GSVAYVPQVSWIFNATVRENILFG----SDFESERYWRAidVTALQHdLDLLPGRDLTEIGERGVNISGGQKQRVSMARA 754
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 496 LLKNAPVVILDEPTAALDIESELAV-QKAIDNLVHNRTVIIIAHRLSTIAGAGNILVIEEGQVVEQGTHAQLLSHHGRYQ 574
Cdd:PLN03232 755 VYSNSDIYIFDDPLSALDAHVAHQVfDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGSLFK 834
|
..
gi 1805558896 575 AL 576
Cdd:PLN03232 835 KL 836
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
344-558 |
2.07e-18 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 88.55 E-value: 2.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 344 IRFDNVSYRYeeGDGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGG--VDIRrlTPEQLNSL- 420
Cdd:COG3845 6 LELRGITKRF--GGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGkpVRIR--SPRDAIALg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 421 ISVVFQDVWLFDD-TLLANIRIARPQATRQEVEEAARAAQCLEFISRLpqGWLTPMGEMGGQLSGGERQRISIARALLKN 499
Cdd:COG3845 82 IGMVHQHFMLVPNlTVAENIVLGLEPTKGGRLDRKAARARIRELSERY--GLDVDPDAKVEDLSVGEQQRVEILKALYRG 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1805558896 500 APVVILDEPTAAL-DIESElAVQKAIDNLVHN-RTVIIIAHRLSTI-AGAGNILVIEEGQVV 558
Cdd:COG3845 160 ARILILDEPTAVLtPQEAD-ELFEILRRLAAEgKSIIFITHKLREVmAIADRVTVLRRGKVV 220
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
344-568 |
3.36e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 85.04 E-value: 3.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 344 IRFDNVSYRYEEGDGhALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLTPEQ-LNSLIS 422
Cdd:PRK13644 2 IRLENVSYSYPDGTP-ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQgIRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 423 VVFQ--DVWLFDDTLLANIRIAR------PQATRQEVEEAARAAQCLEFISRLPQgwltpmgemggQLSGGERQRISIAR 494
Cdd:PRK13644 81 IVFQnpETQFVGRTVEEDLAFGPenlclpPIEIRKRVDRALAEIGLEKYRHRSPK-----------TLSGGQGQCVALAG 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1805558896 495 ALLKNAPVVILDEPTAALDIESELAVQKAIDNLVHN-RTVIIIAHRLSTIAGAGNILVIEEGQVVEQGTHAQLLS 568
Cdd:PRK13644 150 ILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKgKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLS 224
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
348-568 |
4.66e-18 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 84.52 E-value: 4.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 348 NVSYRYEEGDGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADpQQGQISIGGVDIRRLTPEQLNSLISVVFQD 427
Cdd:cd03289 7 DLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKAFGVIPQK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 428 VWLFDDTLLANIRiARPQATRQEVEEAARAAQCLEFISRLPqGWLTPMGEMGGQ-LSGGERQRISIARALLKNAPVVILD 506
Cdd:cd03289 86 VFIFSGTFRKNLD-PYGKWSDEEIWKVAEEVGLKSVIEQFP-GQLDFVLVDGGCvLSHGHKQLMCLARSVLSKAKILLLD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1805558896 507 EPTAALDIESELAVQKAIDNLVHNRTVIIIAHRLSTIAGAGNILVIEEGQVVEQGTHAQLLS 568
Cdd:cd03289 164 EPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLN 225
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
348-568 |
1.08e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 83.17 E-value: 1.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 348 NVSYRYEEGDGHA-LNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGV------DIRRLTPEQLNSL 420
Cdd:PRK14246 12 NISRLYLYINDKAiLKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAIKLRKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 421 ISVVFQD------VWLFDDTL--LANIRIARPQATRQEVEEAARAAQCL-EFISRLpqgwltpmGEMGGQLSGGERQRIS 491
Cdd:PRK14246 92 VGMVFQQpnpfphLSIYDNIAypLKSHGIKEKREIKKIVEECLRKVGLWkEVYDRL--------NSPASQLSGGQQQRLT 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1805558896 492 IARALLKNAPVVILDEPTAALDIESELAVQKAIDNLVHNRTVIIIAHRLSTIAGAGN-ILVIEEGQVVEQGTHAQLLS 568
Cdd:PRK14246 164 IARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARVADyVAFLYNGELVEWGSSNEIFT 241
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
347-569 |
1.48e-17 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 82.96 E-value: 1.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 347 DNVSYRYEEGDG-------HALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGvdiRRLTPE---Q 416
Cdd:COG4167 8 RNLSKTFKYRTGlfrrqqfEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILING---HKLEYGdykY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 417 LNSLISVVFQDVwlfDDTLLANIRIAR----PQATRQEVEEAARAAQCLEFISR---LPQGWLTP--MgemggqLSGGER 487
Cdd:COG4167 85 RCKHIRMIFQDP---NTSLNPRLNIGQileePLRLNTDLTAEEREERIFATLRLvglLPEHANFYphM------LSSGQK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 488 QRISIARALLKNAPVVILDEPTAALDIeselAVQKAIDNLV------HNRTVIIIAHRLSTIAG-AGNILVIEEGQVVEQ 560
Cdd:COG4167 156 QRVALARALILQPKIIIADEALAALDM----SVRSQIINLMlelqekLGISYIYVSQHLGIVKHiSDKVLVMHQGEVVEY 231
|
....*....
gi 1805558896 561 GTHAQLLSH 569
Cdd:COG4167 232 GKTAEVFAN 240
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
361-564 |
1.61e-17 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 86.76 E-value: 1.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 361 LNHVSLTFPAASMSALVGASGAGKTTVTKLLMryadpQQGQISIGGVDIRRLtpeqlnslISVVFQDVWLFDDTLLANIR 440
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLL-----SQFEISEGRVWAERS--------IAYVPQQAWIMNATVRGNIL 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 441 IARPQATrQEVEEAARAAQCLEFISRLPQGWLTPMGEMGGQLSGGERQRISIARALLKNAPVVILDEPTAALDIE-SELA 519
Cdd:PTZ00243 743 FFDEEDA-ARLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHvGERV 821
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1805558896 520 VQKAIDNLVHNRTVIIIAHRLSTIAGAGNILVIEEGQVVEQGTHA 564
Cdd:PTZ00243 822 VEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSA 866
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
356-540 |
2.03e-17 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 82.13 E-value: 2.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 356 GDGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYAD--PQ---QGQISIGGVDI--RRLTPEQLNSLISVVFQDV 428
Cdd:PRK14239 16 NKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnPEvtiTGSIVYNGHNIysPRTDTVDLRKEIGMVFQQP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 429 WLFDDTLLANI----RIA--RPQATRQE-VEEAARAAQCL-EFISRLPQGWLTpmgemggqLSGGERQRISIARALLKNA 500
Cdd:PRK14239 96 NPFPMSIYENVvyglRLKgiKDKQVLDEaVEKSLKGASIWdEVKDRLHDSALG--------LSGGQQQRVCIARVLATSP 167
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1805558896 501 PVVILDEPTAALDIESELAVQKAIDNLVHNRTVIIIAHRL 540
Cdd:PRK14239 168 KIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSM 207
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
359-558 |
2.31e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 82.44 E-value: 2.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 359 HALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLTPEQLNSLISVVFQDVWL---FDDTL 435
Cdd:COG1101 20 RALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAKYIGRVFQDPMMgtaPSMTI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 436 LANIRIA---------RPQATRQEVEEAAraaqclEFISRLPQGwL-----TPMGemggQLSGGERQRISIARALLKNAP 501
Cdd:COG1101 100 EENLALAyrrgkrrglRRGLTKKRRELFR------ELLATLGLG-LenrldTKVG----LLSGGQRQALSLLMATLTKPK 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 502 VVILDEPTAALDIESELAVQKAIDNLV--HNRTVIIIAHRLSTIAGAGN-ILVIEEGQVV 558
Cdd:COG1101 169 LLLLDEHTAALDPKTAALVLELTEKIVeeNNLTTLMVTHNMEQALDYGNrLIMMHEGRII 228
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
361-568 |
2.34e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 82.45 E-value: 2.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 361 LNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADP-----QQGQISIGGVDIRRLTPE-QLNSLISVVFQDVWLFD-- 432
Cdd:PRK14271 37 LDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSIFNYRDVlEFRRRVGMLFQRPNPFPms 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 433 --DTLLANIRiARPQATRQEVEEAARAaqclefisRLPQGWL-----TPMGEMGGQLSGGERQRISIARALLKNAPVVIL 505
Cdd:PRK14271 117 imDNVLAGVR-AHKLVPRKEFRGVAQA--------RLTEVGLwdavkDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLL 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1805558896 506 DEPTAALDIESELAVQKAIDNLVHNRTVIIIAHRLSTIAGAGN-ILVIEEGQVVEQGTHAQLLS 568
Cdd:PRK14271 188 DEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARISDrAALFFDGRLVEEGPTEQLFS 251
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
344-556 |
2.67e-17 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 79.03 E-value: 2.67e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 344 IRFDNVSYRYeeGDGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGgvdirrltpeqlnslisv 423
Cdd:cd03221 1 IELENLSKTY--GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWG------------------ 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 424 vfqdvwlfddtllANIRIArpqatrqeveeaaraaqCLEfisrlpqgwltpmgemggQLSGGERQRISIARALLKNAPVV 503
Cdd:cd03221 61 -------------STVKIG-----------------YFE------------------QLSGGEKMRLALAKLLLENPNLL 92
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1805558896 504 ILDEPTAALDIESELAVQKAIDNlvHNRTVIIIAH-R--LSTIagAGNILVIEEGQ 556
Cdd:cd03221 93 LLDEPTNHLDLESIEALEEALKE--YPGTVILVSHdRyfLDQV--ATKIIELEDGK 144
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
347-557 |
2.68e-17 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 82.03 E-value: 2.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 347 DNVSYRYeeGDGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIrrltpEQLNSLISVVFQ 426
Cdd:PRK11247 16 NAVSKRY--GERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPL-----AEAREDTRLMFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 427 DVWLFD-DTLLANIRIA-----RPQATR--QEVEEAARAaqclefisrlpqgwltpmGEMGGQLSGGERQRISIARALLK 498
Cdd:PRK11247 89 DARLLPwKKVIDNVGLGlkgqwRDAALQalAAVGLADRA------------------NEWPAALSGGQKQRVALARALIH 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1805558896 499 NAPVVILDEPTAALDIESELAVQKAIDNL--VHNRTVIIIAHRLS-TIAGAGNILVIEEGQV 557
Cdd:PRK11247 151 RPGLLLLDEPLGALDALTRIEMQDLIESLwqQHGFTVLLVTHDVSeAVAMADRVLLIEEGKI 212
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
346-538 |
2.84e-17 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 85.12 E-value: 2.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 346 FDNVSYRYeeGDGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISI-GGVDIRRLTPEQL----NSL 420
Cdd:COG0488 1 LENLSKSF--GGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIpKGLRIGYLPQEPPldddLTV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 421 ISVV---FQDVW-----------LFDDTLLANIRIARPQAtrqEVEEA------ARAAQCLefiSRL---PQGWLTPMGE 477
Cdd:COG0488 79 LDTVldgDAELRaleaeleeleaKLAEPDEDLERLAELQE---EFEALggweaeARAEEIL---SGLgfpEEDLDRPVSE 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1805558896 478 mggqLSGGERQRISIARALLKNAPVVILDEPTAALDIESelavqkaID---NLVHNR--TVIIIAH 538
Cdd:COG0488 153 ----LSGGWRRRVALARALLSEPDLLLLDEPTNHLDLES-------IEwleEFLKNYpgTVLVVSH 207
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
349-561 |
3.96e-17 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 81.85 E-value: 3.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 349 VSYRyeegDGH-ALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLTPEQLNSLISVVFQD 427
Cdd:PRK15056 14 VTWR----NGHtALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNLVAYVPQSEEV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 428 VWLF----DDTLLAN-------IRIARPQaTRQEVEEAARAAQCLEFISRlpqgwltpmgeMGGQLSGGERQRISIARAL 496
Cdd:PRK15056 90 DWSFpvlvEDVVMMGryghmgwLRRAKKR-DRQIVTAALARVDMVEFRHR-----------QIGELSGGQKKRVFLARAI 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1805558896 497 LKNAPVVILDEPTAALDIESELAVQKAIDNL-VHNRTVIIIAHRLSTIAGAGNILVIEEGQVVEQG 561
Cdd:PRK15056 158 AQQGQVILLDEPFTGVDVKTEARIISLLRELrDEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASG 223
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
359-561 |
4.73e-17 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 84.52 E-value: 4.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 359 HALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLTPEQLNSL---ISVVFQDVWL-FDDT 434
Cdd:PRK10261 338 HAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALrrdIQFIFQDPYAsLDPR 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 435 LLANIRIARP---QATRQEVEEAARAAQCLEFISRLPQ-GWLTPMgemggQLSGGERQRISIARALLKNAPVVILDEPTA 510
Cdd:PRK10261 418 QTVGDSIMEPlrvHGLLPGKAAAARVAWLLERVGLLPEhAWRYPH-----EFSGGQRQRICIARALALNPKVIIADEAVS 492
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1805558896 511 ALDIeselAVQKAIDNLVHNR------TVIIIAHRLSTIAGAGN-ILVIEEGQVVEQG 561
Cdd:PRK10261 493 ALDV----SIRGQIINLLLDLqrdfgiAYLFISHDMAVVERISHrVAVMYLGQIVEIG 546
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
364-561 |
6.49e-17 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 82.61 E-value: 6.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 364 VSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGG---VDIRR---LTPEQLNslISVVFQDVWLFDD-TLL 436
Cdd:PRK11144 17 VNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvlFDAEKgicLPPEKRR--IGYVFQDARLFPHyKVR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 437 ANIRIArpqATRQEVEEAARAAQCL---EFISRLPqgwltpmgemgGQLSGGERQRISIARALLKNAPVVILDEPTAALD 513
Cdd:PRK11144 95 GNLRYG---MAKSMVAQFDKIVALLgiePLLDRYP-----------GSLSGGEKQRVAIGRALLTAPELLLMDEPLASLD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1805558896 514 IESELAVQKAIDNLVH--NRTVIIIAHRLSTIAG-AGNILVIEEGQVVEQG 561
Cdd:PRK11144 161 LPRKRELLPYLERLAReiNIPILYVSHSLDEILRlADRVVVLEQGKVKAFG 211
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
352-569 |
9.10e-17 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 80.40 E-value: 9.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 352 RYeeGDGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRL----------TPEQLNSL- 420
Cdd:PRK10619 14 RY--GEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVrdkdgqlkvaDKNQLRLLr 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 421 --ISVVFQ--DVWLFDdTLLANIRIARPQA---TRQEVEEaaRAAQCLEFISRLPQGwltpMGEMGGQLSGGERQRISIA 493
Cdd:PRK10619 92 trLTMVFQhfNLWSHM-TVLENVMEAPIQVlglSKQEARE--RAVKYLAKVGIDERA----QGKYPVHLSGGQQQRVSIA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1805558896 494 RALLKNAPVVILDEPTAALDIESELAVQKAIDNLVHN-RTVIIIAHRLSTIAGAGN-ILVIEEGQVVEQGTHAQLLSH 569
Cdd:PRK10619 165 RALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEgKTMVVVTHEMGFARHVSShVIFLHQGKIEEEGAPEQLFGN 242
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
344-513 |
9.83e-17 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 82.05 E-value: 9.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 344 IRFDNVSYRYeeGDGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLTPEQLNslISV 423
Cdd:PRK10851 3 IEIANIKKSF--GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRK--VGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 424 VFQDVWLFDD-TLLANI--------RIARPQ--ATRQEVEEAARAAQCLEFISRLPqgwltpmgemgGQLSGGERQRISI 492
Cdd:PRK10851 79 VFQHYALFRHmTVFDNIafgltvlpRRERPNaaAIKAKVTQLLEMVQLAHLADRYP-----------AQLSGGQKQRVAL 147
|
170 180
....*....|....*....|.
gi 1805558896 493 ARALLKNAPVVILDEPTAALD 513
Cdd:PRK10851 148 ARALAVEPQILLLDEPFGALD 168
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
359-573 |
1.27e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 81.29 E-value: 1.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 359 HALNHVSLTFPAASMSALVGASGAGKTTVTKLL---MRyadPQQGQISIGGVDIRRLTPEQLNSlISVVF---QDVWlFD 432
Cdd:COG4586 36 EAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLtgiLV---PTSGEVRVLGYVPFKRRKEFARR-IGVVFgqrSQLW-WD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 433 ----DTLLANIRIARpqatrqeVEEAaraaqclEFISRLpqGWLTPMGEMGG-------QLSGGERQRISIARALLKNAP 501
Cdd:COG4586 111 lpaiDSFRLLKAIYR-------IPDA-------EYKKRL--DELVELLDLGElldtpvrQLSLGQRMRCELAAALLHRPK 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1805558896 502 VVILDEPTAALDIESELAVQKAIDNLV--HNRTVIIIAHRLSTI-AGAGNILVIEEGQVVEQGTHAQLLSHHGRY 573
Cdd:COG4586 175 ILFLDEPTIGLDVVSKEAIREFLKEYNreRGTTILLTSHDMDDIeALCDRVIVIDHGRIIYDGSLEELKERFGPY 249
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
348-566 |
1.27e-16 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 81.69 E-value: 1.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 348 NVSYRYeeGDGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLTPEQLNslISVVFQD 427
Cdd:PRK11432 11 NITKRF--GSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRD--ICMVFQS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 428 VWLFDD-TLLANI-----RIARPQATR-QEVEEAaraaqcLEFISrlpqgwLTPMGE-MGGQLSGGERQRISIARALLKN 499
Cdd:PRK11432 87 YALFPHmSLGENVgyglkMLGVPKEERkQRVKEA------LELVD------LAGFEDrYVDQISGGQQQRVALARALILK 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 500 APVVILDEPTAALDIESELAVQKAIDNLVH--NRTVIIIAHRLS-TIAGAGNILVIEEGQVVEQGTHAQL 566
Cdd:PRK11432 155 PKVLLFDEPLSNLDANLRRSMREKIRELQQqfNITSLYVTHDQSeAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
361-566 |
1.30e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 82.79 E-value: 1.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 361 LNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLTPEQLNSL-ISVVFQDVWLFDD-TLLAN 438
Cdd:PRK15439 27 LKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLgIYLVPQEPLLFPNlSVKEN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 439 I--RIARPQATRQEVEEAARAAQC-LEFISRlpqgwltpmgemGGQLSGGERQRISIARALLKNAPVVILDEPTAALD-I 514
Cdd:PRK15439 107 IlfGLPKRQASMQKMKQLLAALGCqLDLDSS------------AGSLEVADRQIVEILRGLMRDSRILILDEPTASLTpA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1805558896 515 ESELAVQKAIDNLVHNRTVIIIAHRLSTI-AGAGNILVIEEGQVVEQGTHAQL 566
Cdd:PRK15439 175 ETERLFSRIRELLAQGVGIVFISHKLPEIrQLADRISVMRDGTIALSGKTADL 227
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
338-561 |
1.35e-16 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 82.91 E-value: 1.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 338 MPERYdIRFDNVSYRYeeGDGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLTPEQL 417
Cdd:PRK09700 1 MATPY-ISMAGIGKSF--GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 418 NSL-ISVVFQDVWLFDD-TLLANIRIARpQATRQEV--------EEAARAAQCLefisrLPQGWLTPMGEMGGQLSGGER 487
Cdd:PRK09700 78 AQLgIGIIYQELSVIDElTVLENLYIGR-HLTKKVCgvniidwrEMRVRAAMML-----LRVGLKVDLDEKVANLSISHK 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1805558896 488 QRISIARALLKNAPVVILDEPTAALdIESELAVQKAIDNLVHN--RTVIIIAHRLSTIAGAGN-ILVIEEGQVVEQG 561
Cdd:PRK09700 152 QMLEIAKTLMLDAKVIIMDEPTSSL-TNKEVDYLFLIMNQLRKegTAIVYISHKLAEIRRICDrYTVMKDGSSVCSG 227
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
344-569 |
2.69e-16 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 79.85 E-value: 2.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 344 IRFDNVSYRYeeGDGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLTPeQLNSLISV 423
Cdd:PRK13537 8 IDFRNVEKRY--GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRAR-HARQRVGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 424 VFQdvwlFDD-----TLLANIRIARPQATRQEVEEAARAAQCLEFiSRLPQGWLTPMGEmggqLSGGERQRISIARALLK 498
Cdd:PRK13537 85 VPQ----FDNldpdfTVRENLLVFGRYFGLSAAAARALVPPLLEF-AKLENKADAKVGE----LSGGMKRRLTLARALVN 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1805558896 499 NAPVVILDEPTAALDIESELAVQKAIDNLV-HNRTVIIIAHRLSTIAGAGNIL-VIEEGQVVEQGTHAQLLSH 569
Cdd:PRK13537 156 DPDVLVLDEPTTGLDPQARHLMWERLRSLLaRGKTILLTTHFMEEAERLCDRLcVIEEGRKIAEGAPHALIES 228
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
360-520 |
2.97e-16 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 78.24 E-value: 2.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 360 ALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISI----GGVDIRRLTPEQLNSL----ISVVFQ----- 426
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhdgGWVDLAQASPREILALrrrtIGYVSQflrvi 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 427 ------DVwlfddtllanirIARPQATRQEVEEAA--RAAQCLEFIsRLPQG-W-LTPmgemgGQLSGGERQRISIARAL 496
Cdd:COG4778 106 prvsalDV------------VAEPLLERGVDREEAraRARELLARL-NLPERlWdLPP-----ATFSGGEQQRVNIARGF 167
|
170 180
....*....|....*....|....
gi 1805558896 497 LKNAPVVILDEPTAALDIESELAV 520
Cdd:COG4778 168 IADPPLLLLDEPTASLDAANRAVV 191
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
304-556 |
3.08e-16 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 81.78 E-value: 3.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 304 FI-SYTSVVELIASaLQRIERFM-----AIAPLPVAEQSEMPERYDIRFDNVSYRyeEGDGHAL-NHVSLTFPAASMSAL 376
Cdd:COG4178 318 FVdNYQSLAEWRAT-VDRLAGFEealeaADALPEAASRIETSEDGALALEDLTLR--TPDGRPLlEDLSLSLKPGERLLI 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 377 VGASGAGKTTvtklLMR-------YAdpqQGQIsiggvdirrltpeQLNSLISVVF--QDVWLFDDTLLANirIARPQA- 446
Cdd:COG4178 395 TGPSGSGKST----LLRaiaglwpYG---SGRI-------------ARPAGARVLFlpQRPYLPLGTLREA--LLYPATa 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 447 ---TRQEVEEAARAAQCLEFISRL--PQGWltpmgemGGQLSGGERQRISIARALLKNAPVVILDEPTAALDIESELAVQ 521
Cdd:COG4178 453 eafSDAELREALEAVGLGHLAERLdeEADW-------DQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALY 525
|
250 260 270
....*....|....*....|....*....|....*
gi 1805558896 522 KAIDNLVHNRTVIIIAHRLSTIAGAGNILVIEEGQ 556
Cdd:COG4178 526 QLLREELPGTTVISVGHRSTLAAFHDRVLELTGDG 560
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
332-562 |
4.29e-16 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 79.77 E-value: 4.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 332 VAEQSEMPERYDIRFDNVSYRYEEGDGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYAdPQQGQIS----IGGV 407
Cdd:PRK09473 3 PLAQQQADALLDVKDLRVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLL-AANGRIGgsatFNGR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 408 DIRRLTPEQLNSL----ISVVFQD-------VWLFDDTLLANIRIARPQATRQEVEEAAR---AAQCLEFISRlpqgwlt 473
Cdd:PRK09473 82 EILNLPEKELNKLraeqISMIFQDpmtslnpYMRVGEQLMEVLMLHKGMSKAEAFEESVRmldAVKMPEARKR------- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 474 pMGEMGGQLSGGERQRISIARALLKNAPVVILDEPTAALDIeselAVQKAIDNLVH------NRTVIIIAHRLSTIAG-A 546
Cdd:PRK09473 155 -MKMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDV----TVQAQIMTLLNelkrefNTAIIMITHDLGVVAGiC 229
|
250
....*....|....*.
gi 1805558896 547 GNILVIEEGQVVEQGT 562
Cdd:PRK09473 230 DKVLVMYAGRTMEYGN 245
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
344-568 |
4.95e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 78.54 E-value: 4.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 344 IRFDNVSYRYEEGDghALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQ-----QGQISIGGVDI--RRLTPEQ 416
Cdd:PRK14258 8 IKVNNLSFYYDTQK--ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELEsevrvEGRVEFFNQNIyeRRVNLNR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 417 LNSLISVVFQDVWLFDDTLLANIRIA------RPQATRQEVEEAARAAQCL--EFISRLPQGWLtpmgemggQLSGGERQ 488
Cdd:PRK14258 86 LRRQVSMVHPKPNLFPMSVYDNVAYGvkivgwRPKLEIDDIVESALKDADLwdEIKHKIHKSAL--------DLSGGQQQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 489 RISIARALLKNAPVVILDEPTAALDIESELAVQKAIDNLV--HNRTVIIIAHRLSTIAGAGNILVIEEG------QVVEQ 560
Cdd:PRK14258 158 RLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlrSELTMVIVSHNLHQVSRLSDFTAFFKGnenrigQLVEF 237
|
....*...
gi 1805558896 561 GTHAQLLS 568
Cdd:PRK14258 238 GLTKKIFN 245
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
345-568 |
8.49e-16 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 80.34 E-value: 8.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 345 RFDNVSYRYEegdG-HALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIR-RLTPEQLNSLIS 422
Cdd:PRK11288 6 SFDGIGKTFP---GvKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRfASTTAALAAGVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 423 VVFQDVWLFDD-TLLANIRIARPQATRQEVEEAARAAQCLEFISRL-----PQgwlTPMGEmggqLSGGERQRISIARAL 496
Cdd:PRK11288 83 IIYQELHLVPEmTVAENLYLGQLPHKGGIVNRRLLNYEAREQLEHLgvdidPD---TPLKY----LSIGQRQMVEIAKAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 497 LKNAPVVILDEPTAAL---DIESELAVqkaIDNLVHNRTVII-IAHRLSTI-AGAGNILVIEEGQVVE------QGTHAQ 565
Cdd:PRK11288 156 ARNARVIAFDEPTSSLsarEIEQLFRV---IRELRAEGRVILyVSHRMEEIfALCDAITVFKDGRYVAtfddmaQVDRDQ 232
|
...
gi 1805558896 566 LLS 568
Cdd:PRK11288 233 LVQ 235
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
364-568 |
9.22e-16 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 77.19 E-value: 9.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 364 VSLTFPAASMSALVGASGAGKTTvtkLLMRYAD--PQQGQISIGGVDIRRLTPEQLNSLISVVFQ--------DVWLFDD 433
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKST---LLARMAGllPGQGEILLNGRPLSDWSAAELARHRAYLSQqqsppfamPVFQYLA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 434 TLLAniRIARPQATRQEVEEAARAAQCLEFISRlpqgwltpmgeMGGQLSGGERQRISIARALLKNAPVV-------ILD 506
Cdd:COG4138 92 LHQP--AGASSEAVEQLLAQLAEALGLEDKLSR-----------PLTQLSGGEWQRVRLAAVLLQVWPTInpegqllLLD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1805558896 507 EPTAALDIeselAVQKAIDNLVHN-----RTVIIIAHRLS-TIAGAGNILVIEEGQVVEQGTHAQLLS 568
Cdd:COG4138 159 EPMNSLDV----AQQAALDRLLRElcqqgITVVMSSHDLNhTLRHADRVWLLKQGKLVASGETAEVMT 222
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
344-561 |
9.79e-16 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 76.17 E-value: 9.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 344 IRFDNVSYRYeeGDGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGG-----VDIRRL--TPEQ 416
Cdd:cd03269 1 LEVENVTKRF--GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGkpldiAARNRIgyLPEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 417 LNSLISVVFQDVWLFddtlLANIRIARPQATRQEVEEaaraaqclefisrlpqgWLTPMGEMG------GQLSGGERQRI 490
Cdd:cd03269 79 RGLYPKMKVIDQLVY----LAQLKGLKKEEARRRIDE-----------------WLERLELSEyankrvEELSKGNQQKV 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1805558896 491 SIARALLKNAPVVILDEPTAALDIESELAVQKAIDNLVHN-RTVIIIAHRLSTI-AGAGNILVIEEGQVVEQG 561
Cdd:cd03269 138 QFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARAgKTVILSTHQMELVeELCDRVLLLNKGRAVLYG 210
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
364-513 |
1.07e-15 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 75.98 E-value: 1.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 364 VSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQ---QGQISIGGVDIRRLTPEQLNslISVVFQDVWLFDD-TLLANI 439
Cdd:COG4136 20 LSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALPAEQRR--IGILFQDDLLFPHlSVGENL 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1805558896 440 RIARP-----QATRQEVEEAARAAQCLEFISRLPqgwltpmgemgGQLSGGERQRISIARALLKNAPVVILDEPTAALD 513
Cdd:COG4136 98 AFALPptigrAQRRARVEQALEEAGLAGFADRDP-----------ATLSGGQRARVALLRALLAEPRALLLDEPFSKLD 165
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
347-568 |
1.41e-15 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 76.54 E-value: 1.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 347 DNVSYRYeeGDGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLtPEQLNSLISVVF- 425
Cdd:TIGR04406 5 ENLIKSY--KKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHL-PMHERARLGIGYl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 426 -QDVWLFDD-TLLANIRIA---RPQATRQEVEEaaRAAQCL-EF-ISRLPQgwltpmgEMGGQLSGGERQRISIARALLK 498
Cdd:TIGR04406 82 pQEASIFRKlTVEENIMAVleiRKDLDRAEREE--RLEALLeEFqISHLRD-------NKAMSLSGGERRRVEIARALAT 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1805558896 499 NAPVVILDEPTAALDIESELAVQKAIDNLVH-NRTVIIIAHRL-STIAGAGNILVIEEGQVVEQGTHAQLLS 568
Cdd:TIGR04406 153 NPKFILLDEPFAGVDPIAVGDIKKIIKHLKErGIGVLITDHNVrETLDICDRAYIISDGKVLAEGTPAEIVA 224
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
348-579 |
2.61e-15 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 79.13 E-value: 2.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 348 NVSYRYEEGDGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRR----------LTPEQL 417
Cdd:PRK10261 19 NIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRrsrqvielseQSAAQM 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 418 NSL----ISVVFQD-------VWLFDDTLLANIRIARPQATRQEVEEAARAaqcLEFIsRLPQGWlTPMGEMGGQLSGGE 486
Cdd:PRK10261 99 RHVrgadMAMIFQEpmtslnpVFTVGEQIAESIRLHQGASREEAMVEAKRM---LDQV-RIPEAQ-TILSRYPHQLSGGM 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 487 RQRISIARALLKNAPVVILDEPTAALDIESELAVQKAIDNLVHNRT--VIIIAHRLSTIAG-AGNILVIEEGQVVEQGTH 563
Cdd:PRK10261 174 RQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVVAEiADRVLVMYQGEAVETGSV 253
|
250
....*....|....*...
gi 1805558896 564 AQLL--SHHGRYQALWQA 579
Cdd:PRK10261 254 EQIFhaPQHPYTRALLAA 271
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
347-513 |
3.63e-15 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 75.24 E-value: 3.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 347 DNVSYRYEEGDGHA--LNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLTP----EQLNSL 420
Cdd:PRK11629 9 DNLCKRYQEGSVQTdvLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSaakaELRNQK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 421 ISVVFQDVWLFDD-TLLANIriARP----QATRQEVEEAAR---AAQCLEFISRlpqgwltpmgEMGGQLSGGERQRISI 492
Cdd:PRK11629 89 LGFIYQFHHLLPDfTALENV--AMPlligKKKPAEINSRALemlAAVGLEHRAN----------HRPSELSGGERQRVAI 156
|
170 180
....*....|....*....|.
gi 1805558896 493 ARALLKNAPVVILDEPTAALD 513
Cdd:PRK11629 157 ARALVNNPRLVLADEPTGNLD 177
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
343-568 |
4.24e-15 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 78.21 E-value: 4.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 343 DIRFDNVSYRYEEGDGHALNHVSLTFPAASMSALVGASGAGKtTVTKLLMRYADPQ------QGQISIGGVDIRRLTPEQ 416
Cdd:PRK15134 7 AIENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGK-SVTALSILRLLPSppvvypSGDIRFHGESLLHASEQT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 417 LNSL----ISVVFQDVWLFDDTL----------LANIRIARPQATRQEVeeaaraAQCLEFIS-RLPQGWLTpmgEMGGQ 481
Cdd:PRK15134 86 LRGVrgnkIAMIFQEPMVSLNPLhtlekqlyevLSLHRGMRREAARGEI------LNCLDRVGiRQAAKRLT---DYPHQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 482 LSGGERQRISIARALLKNAPVVILDEPTAALDIeselAVQKAIDNLVH------NRTVIIIAHRLSTIAG-AGNILVIEE 554
Cdd:PRK15134 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDV----SVQAQILQLLRelqqelNMGLLFITHNLSIVRKlADRVAVMQN 232
|
250
....*....|....
gi 1805558896 555 GQVVEQGTHAQLLS 568
Cdd:PRK15134 233 GRCVEQNRAATLFS 246
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
357-546 |
4.49e-15 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 73.81 E-value: 4.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 357 DGH-ALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLTPEQLNslisvvfqdvwlFDDTL 435
Cdd:NF040873 3 GGRpVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQRSE------------VPDSL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 436 LANIRIA-------------RPQAT-RQEVEEAARAAQCLEFISRlpqgwltPMGEmggqLSGGERQRISIARALLKNAP 501
Cdd:NF040873 71 PLTVRDLvamgrwarrglwrRLTRDdRAAVDDALERVGLADLAGR-------QLGE----LSGGQRQRALLAQGLAQEAD 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1805558896 502 VVILDEPTAALDIESELAVQKAIDNLVH-NRTVIIIAHRLSTIAGA 546
Cdd:NF040873 140 LLLLDEPTTGLDAESRERIIALLAEEHArGATVVVVTHDLELVRRA 185
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
361-538 |
7.69e-15 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 74.04 E-value: 7.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 361 LNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLTPEQLnslisVVFQDVWLFD-DTLLANI 439
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM-----VVFQNYSLLPwLTVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 440 RIA----RPQATRQEVEEAARaaQCLEFIsrlpqGWLTPMGEMGGQLSGGERQRISIARALLKNAPVVILDEPTAALDIE 515
Cdd:TIGR01184 76 ALAvdrvLPDLSKSERRAIVE--EHIALV-----GLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDAL 148
|
170 180
....*....|....*....|....*
gi 1805558896 516 SELAVQKAIDNLV--HNRTVIIIAH 538
Cdd:TIGR01184 149 TRGNLQEELMQIWeeHRVTVLMVTH 173
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
359-568 |
8.00e-15 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 77.78 E-value: 8.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 359 HALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADP---QQGQISIGGvdiRRLTPEQLNSLISVVFQDVWLF---- 431
Cdd:TIGR00955 39 HLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNG---MPIDAKEMRAISAYVQQDDLFIptlt 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 432 -DDTLL--ANIRIARPQATRQEVEeaaRAAQCLEFISRLP-QGWLTPMGEMGGQLSGGERQRISIARALLKNAPVVILDE 507
Cdd:TIGR00955 116 vREHLMfqAHLRMPRRVTKKEKRE---RVDEVLQALGLRKcANTRIGVPGRVKGLSGGERKRLAFASELLTDPPLLFCDE 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1805558896 508 PTAALDIESELAVQKAIDNLVHN-RTVIIIAHR-LSTIAGA-GNILVIEEGQVVEQGTHAQLLS 568
Cdd:TIGR00955 193 PTSGLDSFMAYSVVQVLKGLAQKgKTIICTIHQpSSELFELfDKIILMAEGRVAYLGSPDQAVP 256
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
348-568 |
1.11e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 74.73 E-value: 1.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 348 NVSYRYEEGDgHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLTPEQLN--SLISVVF 425
Cdd:PRK13639 6 DLKYSYPDGT-EALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLEvrKTVGIVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 426 QDVwlfDDTLLA------------NIRIARPQATRQeVEEAARAAQCLEFISRLPQgwltpmgemggQLSGGERQRISIA 493
Cdd:PRK13639 85 QNP---DDQLFAptveedvafgplNLGLSKEEVEKR-VKEALKAVGMEGFENKPPH-----------HLSGGQKKRVAIA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1805558896 494 RALLKNAPVVILDEPTAALDIESELAVQKAIDNLvhNR---TVIIIAHRLSTIAG-AGNILVIEEGQVVEQGTHAQLLS 568
Cdd:PRK13639 150 GILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDL--NKegiTIIISTHDVDLVPVyADKVYVMSDGKIIKEGTPKEVFS 226
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
343-579 |
1.35e-14 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 75.33 E-value: 1.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 343 DIRfdNVSYRYEEGDG--HALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQ----QGQISIGGVDIRRLTPEQ 416
Cdd:COG4170 5 DIR--NLTIEIDTPQGrvKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNwhvtADRFRWNGIDLLKLSPRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 417 ----LNSLISVVFQDVWLFDD---TLLANIRIARPQAT------RQEVEEAARAAQCL--------EFIsrlpqgwltpM 475
Cdd:COG4170 83 rrkiIGREIAMIFQEPSSCLDpsaKIGDQLIEAIPSWTfkgkwwQRFKWRKKRAIELLhrvgikdhKDI----------M 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 476 GEMGGQLSGGERQRISIARALLKNAPVVILDEPTAALDIESELAVQKAIDNL--VHNRTVIIIAHRLSTIAG-AGNILVI 552
Cdd:COG4170 153 NSYPHELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLnqLQGTSILLISHDLESISQwADTITVL 232
|
250 260
....*....|....*....|....*....
gi 1805558896 553 EEGQVVEQGTHAQLLS--HHGRYQALWQA 579
Cdd:COG4170 233 YCGQTVESGPTEQILKspHHPYTKALLRS 261
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
344-568 |
1.49e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 74.74 E-value: 1.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 344 IRFDNVSYRYEEG---DGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLTP------ 414
Cdd:PRK13651 3 IKVKNIVKIFNKKlptELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKtkekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 415 ------------------EQLNSLISVVFQ--DVWLFDDTLLANIrIARPQATRQEVEEA-ARAAQCLEFISrLPQGWL- 472
Cdd:PRK13651 83 vleklviqktrfkkikkiKEIRRRVGVVFQfaEYQLFEQTIEKDI-IFGPVSMGVSKEEAkKRAAKYIELVG-LDESYLq 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 473 -TPMGemggqLSGGERQRISIARALLKNAPVVILDEPTAALDIESELAVQKAIDNLVHN-RTVIIIAHRL-STIAGAGNI 549
Cdd:PRK13651 161 rSPFE-----LSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQgKTIILVTHDLdNVLEWTKRT 235
|
250
....*....|....*....
gi 1805558896 550 LVIEEGQVVEQGTHAQLLS 568
Cdd:PRK13651 236 IFFKDGKIIKDGDTYDILS 254
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
364-568 |
1.73e-14 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 73.39 E-value: 1.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 364 VSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLT-PEQLNSLISVVFQDVWLFD-----DTLLA 437
Cdd:PRK10895 22 VSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPlHARARRGIGYLPQEASIFRrlsvyDNLMA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 438 NIRIaRPQATRQEVEEaaRAAQCLE--FISRLPQgwltpmgEMGGQLSGGERQRISIARALLKNAPVVILDEPTAALDIE 515
Cdd:PRK10895 102 VLQI-RDDLSAEQRED--RANELMEefHIEHLRD-------SMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPI 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1805558896 516 SELAVQKAIDNLV-HNRTVIIIAHRL-STIAGAGNILVIEEGQVVEQGTHAQLLS 568
Cdd:PRK10895 172 SVIDIKRIIEHLRdSGLGVLITDHNVrETLAVCERAYIVSQGHLIAHGTPTEILQ 226
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
344-568 |
3.30e-14 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 73.10 E-value: 3.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 344 IRFDNVSYRYeeGDGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLTPEQLNSLISV 423
Cdd:PRK10253 8 LRGEQLTLGY--GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 424 VFQDVWLFDDTLLANIrIAR------PQATR--QEVEEAARAAQCLEFISRLPqgwltpmGEMGGQLSGGERQRISIARA 495
Cdd:PRK10253 86 LAQNATTPGDITVQEL-VARgryphqPLFTRwrKEDEEAVTKAMQATGITHLA-------DQSVDTLSGGQRQRAWIAMV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1805558896 496 LLKNAPVVILDEPTAALDIESELAVQKAIDNLvhNR----TVIIIAHRLSTIAG-AGNILVIEEGQVVEQGTHAQLLS 568
Cdd:PRK10253 158 LAQETAIMLLDEPTTWLDISHQIDLLELLSEL--NRekgyTLAAVLHDLNQACRyASHLIALREGKIVAQGAPKEIVT 233
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
344-562 |
3.52e-14 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 75.22 E-value: 3.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 344 IRFDNVSYRYEegDGHALNHVSLTFPAASMSALVGASGAGKTTVTKLL--MRYADPQQGQI--------SIGGVDI---- 409
Cdd:TIGR03269 1 IEVKNLTKKFD--GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgMDQYEPTSGRIiyhvalceKCGYVERpskv 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 410 --------RRLTPEQ-------------LNSLISVVFQDVWLF--DDTLLANIRIARPQATRQEVEEAARAAQCLEFISR 466
Cdd:TIGR03269 79 gepcpvcgGTLEPEEvdfwnlsdklrrrIRKRIAIMLQRTFALygDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 467 LPQgwltpMGEMGGQLSGGERQRISIARALLKNAPVVILDEPTAALDIESELAVQKAIDNLVHNR--TVIIIAHRLSTIA 544
Cdd:TIGR03269 159 SHR-----ITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASgiSMVLTSHWPEVIE 233
|
250
....*....|....*....
gi 1805558896 545 G-AGNILVIEEGQVVEQGT 562
Cdd:TIGR03269 234 DlSDKAIWLENGEIKEEGT 252
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
344-558 |
3.79e-14 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 75.36 E-value: 3.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 344 IRFDNVSYRYeeGDGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGG------VDIRR--LTPE 415
Cdd:TIGR03719 323 IEAENLTKAF--GDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGEtvklayVDQSRdaLDPN 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 416 QlnslisVVFQDVWLFDDTLLANiriarpqatrqEVEEAARAaqcleFISRLP-QGwlTPMGEMGGQLSGGERQRISIAR 494
Cdd:TIGR03719 401 K------TVWEEISGGLDIIKLG-----------KREIPSRA-----YVGRFNfKG--SDQQKKVGQLSGGERNRVHLAK 456
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1805558896 495 ALLKNAPVVILDEPTAALDIESELAVQKAIDNLVHnrTVIIIAH------RLSTiagagNILVIE-EGQVV 558
Cdd:TIGR03719 457 TLKSGGNVLLLDEPTNDLDVETLRALEEALLNFAG--CAVVISHdrwfldRIAT-----HILAFEgDSHVE 520
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
376-562 |
6.04e-14 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 71.67 E-value: 6.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 376 LVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRrLTPEQLNSLISVVFQDvwlfddtLLANIrIARPQATRQEVEEAA 455
Cdd:cd03237 30 ILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVS-YKPQYIKADYEGTVRD-------LLSSI-TKDFYTHPYFKTEIA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 456 RAAQcLEFI--SRLPQgwltpmgemggqLSGGERQRISIARALLKNAPVVILDEPTAALDIESELAVQKAIDNLV--HNR 531
Cdd:cd03237 101 KPLQ-IEQIldREVPE------------LSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAenNEK 167
|
170 180 190
....*....|....*....|....*....|.
gi 1805558896 532 TVIIIAHRLSTIAGAGNILVIEEGQVVEQGT 562
Cdd:cd03237 168 TAFVVEHDIIMIDYLADRLIVFEGEPSVNGV 198
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
352-561 |
9.16e-14 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 70.25 E-value: 9.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 352 RYEEGDGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQ--QGQISIGGVDIRRLTPEQLNSL-ISVVFQdv 428
Cdd:cd03217 7 HVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYEvtEGEILFKGEDITDLPPEERARLgIFLAFQ-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 429 wlfddtllaniriaRPQatrqEVEEAARAaqclEFISRLPQGwltpmgemggqLSGGERQRISIARALLKNAPVVILDEP 508
Cdd:cd03217 85 --------------YPP----EIPGVKNA----DFLRYVNEG-----------FSGGEKKRNEILQLLLLEPDLAILDEP 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1805558896 509 TAALDIESELAVQKAIDNLVH-NRTVIIIAHRlstiagaGNIL---------VIEEGQVVEQG 561
Cdd:cd03217 132 DSGLDIDALRLVAEVINKLREeGKSVLIITHY-------QRLLdyikpdrvhVLYDGRIVKSG 187
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
360-538 |
1.12e-13 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 71.27 E-value: 1.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 360 ALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLTPEQlnsliSVVFQDVWLFD-DTLLAN 438
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER-----GVVFQNEGLLPwRNVQDN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 439 IRIARPQATRQEVEEAARAAQCL------EFISRLPqgWltpmgemggQLSGGERQRISIARALLKNAPVVILDEPTAAL 512
Cdd:PRK11248 91 VAFGLQLAGVEKMQRLEIAHQMLkkvgleGAEKRYI--W---------QLSGGQRQRVGIARALAANPQLLLLDEPFGAL 159
|
170 180
....*....|....*....|....*...
gi 1805558896 513 DIESELAVQKAIDNLVHN--RTVIIIAH 538
Cdd:PRK11248 160 DAFTREQMQTLLLKLWQEtgKQVLLITH 187
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
344-572 |
1.41e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 71.68 E-value: 1.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 344 IRFDNVSYRYeeGDGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLT-------PEQ 416
Cdd:COG4152 2 LELKGLTKRF--GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDrrrigylPEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 417 --LNSLISVvfQDVWLFddtlLANIRiarpQATRQEVEEAARAaqclefisrlpqgWLTPMGeMGG-------QLSGGER 487
Cdd:COG4152 80 rgLYPKMKV--GEQLVY----LARLK----GLSKAEAKRRADE-------------WLERLG-LGDrankkveELSKGNQ 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 488 QRISIARALLKNAPVVILDEPTAALD-IESELaVQKAIDNLVHN-RTVIIIAHRLSTI-AGAGNILVIEEGQVVEQGTHA 564
Cdd:COG4152 136 QKVQLIAALLHDPELLILDEPFSGLDpVNVEL-LKDVIRELAAKgTTVIFSSHQMELVeELCDRIVIINKGRKVLSGSVD 214
|
....*...
gi 1805558896 565 QLLSHHGR 572
Cdd:COG4152 215 EIRRQFGR 222
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
351-568 |
1.42e-13 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 71.19 E-value: 1.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 351 YRYEegDGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGG--VDIRRLTPEQLNSLISVVFQD- 427
Cdd:PRK13638 9 FRYQ--DEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGkpLDYSKRGLLALRQQVATVFQDp 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 428 ---VWLFD-DTLLA----NIRIARPQATRQeVEEAARAAQCLEFISRLPQGwltpmgemggqLSGGERQRISIARALLKN 499
Cdd:PRK13638 87 eqqIFYTDiDSDIAfslrNLGVPEAEITRR-VDEALTLVDAQHFRHQPIQC-----------LSHGQKKRVAIAGALVLQ 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1805558896 500 APVVILDEPTAALDIESELAVQKAIDNLV-HNRTVIIIAHRLSTIAGAGN-ILVIEEGQVVEQGTHAQLLS 568
Cdd:PRK13638 155 ARYLLLDEPTAGLDPAGRTQMIAIIRRIVaQGNHVIISSHDIDLIYEISDaVYVLRQGQILTHGAPGEVFA 225
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
377-543 |
1.67e-13 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 73.28 E-value: 1.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 377 VGASGAGKTTVTKLLMRYADPQQGQISiGGVDI----RRLTPEQ-------LNSLISVVFQDVWLFDDtllanirIARP- 444
Cdd:COG1245 372 VGPNGIGKTTFAKILAGVLKPDEGEVD-EDLKIsykpQYISPDYdgtveefLRSANTDDFGSSYYKTE-------IIKPl 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 445 QATR---QEVEEaaraaqclefisrlpqgwltpmgemggqLSGGERQRISIARALLKNAPVVILDEPTAALDIESELAVQ 521
Cdd:COG1245 444 GLEKlldKNVKD----------------------------LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVA 495
|
170 180
....*....|....*....|....
gi 1805558896 522 KAIDNLVHNR--TVIIIAHRLSTI 543
Cdd:COG1245 496 KAIRRFAENRgkTAMVVDHDIYLI 519
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
356-561 |
1.97e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 70.64 E-value: 1.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 356 GDGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQ-----GQISIGGVDI--RRLTPEQLNSLISVVFQDV 428
Cdd:PRK14267 15 GSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEearveGEVRLFGRNIysPDVDPIEVRREVGMVFQYP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 429 WLFDD-TLLANIRI-------ARPQATRQEVEEAA--RAAQCLEFISRLpqgwltpmGEMGGQLSGGERQRISIARALLK 498
Cdd:PRK14267 95 NPFPHlTIYDNVAIgvklnglVKSKKELDERVEWAlkKAALWDEVKDRL--------NDYPSNLSGGQRQRLVIARALAM 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1805558896 499 NAPVVILDEPTAALDIESELAVQKAIDNLVHNRTVIIIAHRLSTIAGAGN-ILVIEEGQVVEQG 561
Cdd:PRK14267 167 KPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAQAARVSDyVAFLYLGKLIEVG 230
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
331-562 |
2.56e-13 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 73.51 E-value: 2.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 331 PVAEQSEMPER----YDIRFD-------------NVSYRYEEGDGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMR 393
Cdd:TIGR01257 899 PLTEEMEDPEHpegiNDSFFErelpglvpgvcvkNLVKIFEPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTG 978
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 394 YADPQQGQISIGGVDIRRlTPEQLNSLISVVFQDVWLFDDTLLANIRIARPQATRQEVEEAAraaqcLEFISRLPQ-GWL 472
Cdd:TIGR01257 979 LLPPTSGTVLVGGKDIET-NLDAVRQSLGMCPQHNILFHHLTVAEHILFYAQLKGRSWEEAQ-----LEMEAMLEDtGLH 1052
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 473 TPMGEMGGQLSGGERQRISIARALLKNAPVVILDEPTAALDIESELAVQKAIDNLVHNRTVIIIAHRLSTIAGAGN-ILV 551
Cdd:TIGR01257 1053 HKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADLLGDrIAI 1132
|
250
....*....|.
gi 1805558896 552 IEEGQVVEQGT 562
Cdd:TIGR01257 1133 ISQGRLYCSGT 1143
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
361-562 |
5.50e-13 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 68.94 E-value: 5.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 361 LNHVSLTFPAASMSALVGASGAGKTTVTKLLM---RYaDPQQGQISIGGVDIRRLTPEQLNSL-ISVVFQD--------V 428
Cdd:COG0396 16 LKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMghpKY-EVTSGSILLDGEDILELSPDERARAgIFLAFQYpveipgvsV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 429 WLFDDTLLANIRIARPQAT--RQEVEEAARAaqcL----EFISRlpqgwltpmgEMGGQLSGGERQRISIARALLKNAPV 502
Cdd:COG0396 95 SNFLRTALNARRGEELSARefLKLLKEKMKE---LgldeDFLDR----------YVNEGFSGGEKKRNEILQMLLLEPKL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1805558896 503 VILDEPTAALDIESELAVQKAIDNLVH-NRTVIIIAH--RLSTIAGAGNILVIEEGQVVEQGT 562
Cdd:COG0396 162 AILDETDSGLDIDALRIVAEGVNKLRSpDRGILIITHyqRILDYIKPDFVHVLVDGRIVKSGG 224
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
360-556 |
5.69e-13 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 71.50 E-value: 5.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 360 ALNHVSLTFPAASMSALVGASGAGKTTVTKLL---MRYADpQQGQISIGGVDIR----RLTpEQLNslISVVFQDVWLFD 432
Cdd:PRK13549 20 ALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLsgvYPHGT-YEGEIIFEGEELQasniRDT-ERAG--IAIIHQELALVK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 433 D-TLLANIRIARPQATRQEVEEAARAAQCLEFISRL-----PQgwlTPMGEMGGqlsgGERQRISIARALLKNAPVVILD 506
Cdd:PRK13549 96 ElSVLENIFLGNEITPGGIMDYDAMYLRAQKLLAQLkldinPA---TPVGNLGL----GQQQLVEIAKALNKQARLLILD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1805558896 507 EPTAALdIESELAVQKAI--DNLVHNRTVIIIAHRLSTIAG-AGNILVIEEGQ 556
Cdd:PRK13549 169 EPTASL-TESETAVLLDIirDLKAHGIACIYISHKLNEVKAiSDTICVIRDGR 220
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
344-507 |
6.73e-13 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 71.16 E-value: 6.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 344 IRFDNVSYRYEEGdGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLTPEQLNSLISV 423
Cdd:PRK10522 323 LELRNVTFAYQDN-GFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSA 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 424 VFQDVWLFDDTLlaniriaRPQAtrqEVEEAARAAQCLEFIS-----RLPQGWLTPMgemggQLSGGERQRISIARALLK 498
Cdd:PRK10522 402 VFTDFHLFDQLL-------GPEG---KPANPALVEKWLERLKmahklELEDGRISNL-----KLSKGQKKRLALLLALAE 466
|
....*....
gi 1805558896 499 NAPVVILDE 507
Cdd:PRK10522 467 ERDILLLDE 475
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
361-560 |
7.79e-13 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 68.27 E-value: 7.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 361 LNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLTPEQLNSL----ISVVFQDVWLFDdTLL 436
Cdd:PRK10584 26 LTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLrakhVGFVFQSFMLIP-TLN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 437 ANIRIARPQATRQEVEEAARAaQCLEFISRLPQGwlTPMGEMGGQLSGGERQRISIARALLKNAPVVILDEPTAALDIES 516
Cdd:PRK10584 105 ALENVELPALLRGESSRQSRN-GAKALLEQLGLG--KRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQT 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1805558896 517 ElavQKAID-----NLVHNRTVIIIAHRLSTIAGAGNILVIEEGQVVEQ 560
Cdd:PRK10584 182 G---DKIADllfslNREHGTTLILVTHDLQLAARCDRRLRLVNGQLQEE 227
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
482-543 |
7.99e-13 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 71.38 E-value: 7.99e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1805558896 482 LSGGERQRISIARALLKNAPVVILDEPTAALDIESELAVQKAIDNLVHNR--TVIIIAHRLSTI 543
Cdd:PRK13409 454 LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEEReaTALVVDHDIYMI 517
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
482-565 |
1.19e-12 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 66.44 E-value: 1.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 482 LSGGERQRISIARALLKNAPVVILDEPTAALDIESELAVQKAIDNLVHN--RTVIIIAHRLSTIAGAGNILVIEEGQVVE 559
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEgkKTALVVEHDLAVLDYLSDRIHVFEGEPGV 151
|
....*.
gi 1805558896 560 QGTHAQ 565
Cdd:cd03222 152 YGIASQ 157
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
344-569 |
1.49e-12 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 67.60 E-value: 1.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 344 IRFDNVSYRYeeGDGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRL-TPEQLNSLIS 422
Cdd:PRK11614 6 LSFDKVSAHY--GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWqTAKIMREAVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 423 VVFQDVWLFDD-TLLANIRIARPQATRQEVEEaaRAAQCLEFISRLPQGWLTPMGEMggqlSGGERQRISIARALLKNAP 501
Cdd:PRK11614 84 IVPEGRRVFSRmTVEENLAMGGFFAERDQFQE--RIKWVYELFPRLHERRIQRAGTM----SGGEQQMLAIGRALMSQPR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1805558896 502 VVILDEPTAALdieSELAVQKAIDNLVHNR----TVIII---AHRLSTIAGAGniLVIEEGQVVEQGTHAQLLSH 569
Cdd:PRK11614 158 LLLLDEPSLGL---APIIIQQIFDTIEQLReqgmTIFLVeqnANQALKLADRG--YVLENGHVVLEDTGDALLAN 227
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
344-540 |
1.61e-12 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 67.83 E-value: 1.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 344 IRFDNVSYRYeeGDGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQIsiggvdirrLTPEQLNslISV 423
Cdd:PRK09544 5 VSLENVSVSF--GQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI---------KRNGKLR--IGY 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 424 VFQDVWLfDDTL---LANIRIARPQATRQEVEEA---ARAAQCLEFisrlpqgwltPMGemggQLSGGERQRISIARALL 497
Cdd:PRK09544 72 VPQKLYL-DTTLpltVNRFLRLRPGTKKEDILPAlkrVQAGHLIDA----------PMQ----KLSGGETQRVLLARALL 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1805558896 498 KNAPVVILDEPTAALDIESELAVQKAIDNLVH--NRTVIIIAHRL 540
Cdd:PRK09544 137 NRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRelDCAVLMVSHDL 181
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
481-540 |
1.76e-12 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 70.22 E-value: 1.76e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 481 QLSGGERQRISIARALLKNAPVVILDEPTAALDIESELAVQKAIDNLVHNRTVIIIAHRL 540
Cdd:PRK13409 212 ELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIRELAEGKYVLVVEHDL 271
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
347-579 |
2.44e-12 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 68.23 E-value: 2.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 347 DNVSYRYEEGDghalnhvsltfpaasMSALVGASGAGKTTVTKLLMRYAD-P---QQGQISIGGVDIRRLTPEQLNSLI- 421
Cdd:PRK11022 24 DRISYSVKQGE---------------VVGIVGESGSGKSVSSLAIMGLIDyPgrvMAEKLEFNGQDLQRISEKERRNLVg 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 422 ---SVVFQD-VWLFDDTLLANIRIARPQATRQEVEEAARAAQCLEFISRLpqGWLTPMGEMG---GQLSGGERQRISIAR 494
Cdd:PRK11022 89 aevAMIFQDpMTSLNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQV--GIPDPASRLDvypHQLSGGMSQRVMIAM 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 495 ALLKNAPVVILDEPTAALD-------IESELAVQKAidnlvHNRTVIIIAHRLSTIA-GAGNILVIEEGQVVEQGTHAQL 566
Cdd:PRK11022 167 AIACRPKLLIADEPTTALDvtiqaqiIELLLELQQK-----ENMALVLITHDLALVAeAAHKIIVMYAGQVVETGKAHDI 241
|
250
....*....|....*
gi 1805558896 567 LS--HHGRYQALWQA 579
Cdd:PRK11022 242 FRapRHPYTQALLRA 256
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
344-513 |
3.16e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 67.93 E-value: 3.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 344 IRFDNVSYRYeeGDGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIrrltPEQLNSL--- 420
Cdd:PRK13536 42 IDLAGVSKSY--GDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPV----PARARLArar 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 421 ISVVFQdvwlFD---------DTLLANIRIARPQAtrQEVEEAAraAQCLEFiSRLPQGWLTPMGEmggqLSGGERQRIS 491
Cdd:PRK13536 116 IGVVPQ----FDnldleftvrENLLVFGRYFGMST--REIEAVI--PSLLEF-ARLESKADARVSD----LSGGMKRRLT 182
|
170 180
....*....|....*....|..
gi 1805558896 492 IARALLKNAPVVILDEPTAALD 513
Cdd:PRK13536 183 LARALINDPQLLILDEPTTGLD 204
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
343-579 |
3.48e-12 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 67.91 E-value: 3.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 343 DIRFDNVSYRYEEGDGHALNHVSLTFPAASMSALVGASGAGKTTVTKLL--------------MRYADpqqgqisiggVD 408
Cdd:PRK15093 5 DIRNLTIEFKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAIcgvtkdnwrvtadrMRFDD----------ID 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 409 IRRLTPEQLNSLI----SVVFQDVwlfDDTLLANIRIAR------PQAT-----RQEVEEAARAAqcLEFISRLP-QGWL 472
Cdd:PRK15093 75 LLRLSPRERRKLVghnvSMIFQEP---QSCLDPSERVGRqlmqniPGWTykgrwWQRFGWRKRRA--IELLHRVGiKDHK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 473 TPMGEMGGQLSGGERQRISIARALLKNAPVVILDEPTAALDIESELAVQKAIDNLVHNR--TVIIIAHRLSTIAG-AGNI 549
Cdd:PRK15093 150 DAMRSFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNntTILLISHDLQMLSQwADKI 229
|
250 260 270
....*....|....*....|....*....|..
gi 1805558896 550 LVIEEGQVVEQGTHAQLLS--HHGRYQALWQA 579
Cdd:PRK15093 230 NVLYCGQTVETAPSKELVTtpHHPYTQALIRA 261
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
355-517 |
3.51e-12 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 65.59 E-value: 3.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 355 EGDGHAL-NHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLTPEQLNSLISVVFQDVWLFDD 433
Cdd:cd03231 9 ERDGRALfSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 434 TLLANIRIARPQATRQEVEEAaraaqclefisrLPQGWLTPMGEMG-GQLSGGERQRISIARALLKNAPVVILDEPTAAL 512
Cdd:cd03231 89 SVLENLRFWHADHSDEQVEEA------------LARVGLNGFEDRPvAQLSAGQQRRVALARLLLSGRPLWILDEPTTAL 156
|
....*
gi 1805558896 513 DIESE 517
Cdd:cd03231 157 DKAGV 161
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
352-539 |
5.42e-12 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 65.75 E-value: 5.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 352 RYEEGDGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQisiGGVDIRRLTPEQLNSLIsvvfQDVWLF 431
Cdd:COG2401 37 ELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVA---GCVDVPDNQFGREASLI----DAIGRK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 432 DDTLLAniriarpqatrqeveeaaraaqcLEFISRL----PQGWLTPMGEmggqLSGGERQRISIARALLKNAPVVILDE 507
Cdd:COG2401 110 GDFKDA-----------------------VELLNAVglsdAVLWLRRFKE----LSTGQKFRFRLALLLAERPKLLVIDE 162
|
170 180 190
....*....|....*....|....*....|....
gi 1805558896 508 PTAALDIESELAVQKAIDNLV--HNRTVIIIAHR 539
Cdd:COG2401 163 FCSHLDRQTAKRVARNLQKLArrAGITLVVATHH 196
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
343-561 |
7.79e-12 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 66.98 E-value: 7.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 343 DIRFDNVSYRYeeGDGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLTPEQLNslIS 422
Cdd:PRK11000 3 SVTLRNVTKAY--GDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERG--VG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 423 VVFQDVWLFDDTLLAN-----IRIARPQAT--RQEVEEAARAAQCLEFISRLPQGwltpmgemggqLSGGERQRISIARA 495
Cdd:PRK11000 79 MVFQSYALYPHLSVAEnmsfgLKLAGAKKEeiNQRVNQVAEVLQLAHLLDRKPKA-----------LSGGQRQRVAIGRT 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1805558896 496 LLKNAPVVILDEPTAALDieSELAVQKAID-NLVH---NRTVIIIAH-RLSTIAGAGNILVIEEGQVVEQG 561
Cdd:PRK11000 148 LVAEPSVFLLDEPLSNLD--AALRVQMRIEiSRLHkrlGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVG 216
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
364-516 |
1.52e-11 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 63.92 E-value: 1.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 364 VSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLTPEQLNSLISVVFQDVWLFDDTLLANIRI-A 442
Cdd:TIGR01189 19 LSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPGLKPELSALENLHFwA 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1805558896 443 RPQATRQEVEEAARAAQCLEFISRLPqgwltpmgemGGQLSGGERQRISIARALLKNAPVVILDEPTAALDIES 516
Cdd:TIGR01189 99 AIHGGAQRTIEDALAAVGLTGFEDLP----------AAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAG 162
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
358-557 |
1.75e-11 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 63.22 E-value: 1.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 358 GHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLTPEQlnslisvvfqdvwlfddtlla 437
Cdd:cd03215 13 KGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRD--------------------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 438 niRIARPQAtrqeveeaaraaqcleFIS--RLPQGWLTPMG-----EMGGQLSGGERQRISIARALLKNAPVVILDEPTA 510
Cdd:cd03215 72 --AIRAGIA----------------YVPedRKREGLVLDLSvaeniALSSLLSGGNQQKVVLARWLARDPRVLILDEPTR 133
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1805558896 511 ALDIESELAVQKAIDNLV-HNRTVIIIAHRLSTIAG-AGNILVIEEGQV 557
Cdd:cd03215 134 GVDVGAKAEIYRLIRELAdAGKAVLLISSELDELLGlCDRILVMYEGRI 182
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
53-321 |
2.07e-11 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 65.22 E-value: 2.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 53 PIIDALLRGDAPQ-----LLNWAMAFSVAAIVTLVLRWYglgfeyRGHL-----AQATHELRLRLGEQLRRVPLEKLQRG 122
Cdd:cd18563 24 ILIDDVLIQLGPGgntslLLLLVLGLAGAYVLSALLGIL------RGRLlarlgERITADLRRDLYEHLQRLSLSFFDKR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 123 RAGEMNALLLGSVDeNLNYVIA------IANILLLTIVtpltaSLATLWIDWRLGLVMLLIFPLLVPFYYWRRPAMRRQM 196
Cdd:cd18563 98 QTGSLMSRVTSDTD-RLQDFLSdglpdfLTNILMIIGI-----GVVLFSLNWKLALLVLIPVPLVVWGSYFFWKKIRRLF 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 197 QTLGEAHQRLSGDIVEFAQGMMVLRTCGSDADKSRALLAHFNALENLQTRTHRQGAGATMLIASVVELGLQVVVLSGIVW 276
Cdd:cd18563 172 HRQWRRWSRLNSVLNDTLPGIRVVKAFGQEKREIKRFDEANQELLDANIRAEKLWATFFPLLTFLTSLGTLIVWYFGGRQ 251
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1805558896 277 VVTGTLNLAFLIAAVAMIMRFAEPMAMFISYTSVVELIASALQRI 321
Cdd:cd18563 252 VLSGTMTLGTLVAFLSYLGMFYGPLQWLSRLNNWITRALTSAERI 296
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
319-538 |
2.71e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 66.51 E-value: 2.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 319 QRIERfMAIAPLPVAEQSEMPErydIRFD--NVSYRYeeGDGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYAD 396
Cdd:PRK11147 297 ERREV-MGTAKMQVEEASRSGK---IVFEmeNVNYQI--DGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQ 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 397 PQQGQISIGG------VDIRR--LTPEQlnslisvvfqdvwlfddTLLANIriarpQATRQEVEEAARAAQCLEFIsrlp 468
Cdd:PRK11147 371 ADSGRIHCGTklevayFDQHRaeLDPEK-----------------TVMDNL-----AEGKQEVMVNGRPRHVLGYL---- 424
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1805558896 469 QGWL-TPMGEMG--GQLSGGERQRISIARALLKNAPVVILDEPTAALDIES-ELaVQKAIDNlvHNRTVIIIAH 538
Cdd:PRK11147 425 QDFLfHPKRAMTpvKALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETlEL-LEELLDS--YQGTVLLVSH 495
|
|
| ABC_6TM_AarD_CydD |
cd18584 |
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH ... |
34-221 |
2.83e-11 |
|
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH transporter, and a homolog AarD; The CydD protein, together with the CydC protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350028 [Multi-domain] Cd Length: 290 Bit Score: 64.74 E-value: 2.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 34 MLALLLAAFMqgIAFA-CLYPIIDALLRGDAP--QLLNWAMAFSVAAIVTLVLRWYGlgfEYRGHLA--QATHELRLRLG 108
Cdd:cd18584 3 LLGLLAALLI--IAQAwLLARIIAGVFLEGAGlaALLPLLLLLLAALLLRALLAWAQ---ERLAARAaaRVKAELRRRLL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 109 EQLRRVPLEKLQRGRAGEMNALLLGSVDENLNYVIAIANILLLTIVTPLTASLATLWIDWRLGLVMLLIFPlLVPFYYW- 187
Cdd:cd18584 78 ARLLALGPALLRRQSSGELATLLTEGVDALDGYFARYLPQLVLAAIVPLLILVAVFPLDWVSALILLVTAP-LIPLFMIl 156
|
170 180 190
....*....|....*....|....*....|....*...
gi 1805558896 188 ----RRPAMRRQMQTLgeahQRLSGDIVEFAQGMMVLR 221
Cdd:cd18584 157 igkaAQAASRRQWAAL----SRLSGHFLDRLRGLPTLK 190
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
344-566 |
3.20e-11 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 64.26 E-value: 3.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 344 IRFDNVSYRYEEGdgHALNHVSLTFPAASMSALVGASGAGKTTVTKLL--MRYADPQQG-QISIGGVDIRRLTP-----E 415
Cdd:PRK09984 5 IRVEKLAKTFNQH--QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLsgLITGDKSAGsHIELLGRTVQREGRlardiR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 416 QLNSLISVVFQDVWLFDD-TLLANIRIARPQATrqeveeaARAAQCLEFISRL-PQGWLTPMGEMG---------GQLSG 484
Cdd:PRK09984 83 KSRANTGYIFQQFNLVNRlSVLENVLIGALGST-------PFWRTCFSWFTREqKQRALQALTRVGmvhfahqrvSTLSG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 485 GERQRISIARALLKNAPVVILDEPTAALDIESELAVQKAIDNLVHNR--TVIIIAHRLS-TIAGAGNILVIEEGQVVEQG 561
Cdd:PRK09984 156 GQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDgiTVVVTLHQVDyALRYCERIVALRQGHVFYDG 235
|
....*
gi 1805558896 562 THAQL 566
Cdd:PRK09984 236 SSQQF 240
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
480-542 |
3.25e-11 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 65.96 E-value: 3.25e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1805558896 480 GQLSGGERQRISIARALLKNAPVVILDEPTAALDIESELAVQKAIDNLV-HNRTVIIIAHRLST 542
Cdd:COG1245 211 SELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLNVARLIRELAeEGKYVLVVEHDLAI 274
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
356-558 |
3.82e-11 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 65.62 E-value: 3.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 356 GDGHALNHVSLTFPAASMSALVGASGAGKTTVTKLL--MRYADPQQGQISIGGVDIR-RLTPEQLNSLISVVFQDVWLFD 432
Cdd:TIGR02633 12 GGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILsgVYPHGTWDGEIYWSGSPLKaSNIRDTERAGIVIIHQELTLVP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 433 D-TLLANI----RIARPqATRQEVEEAARAAQCLEFISRLPqgwLTPMGEMGGQLSGGERQRISIARALLKNAPVVILDE 507
Cdd:TIGR02633 92 ElSVAENIflgnEITLP-GGRMAYNAMYLRAKNLLRELQLD---ADNVTRPVGDYGGGQQQLVEIAKALNKQARLLILDE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1805558896 508 PTAAL-DIESELAVQKAIDNLVHNRTVIIIAHRLSTIAGAGN-ILVIEEGQVV 558
Cdd:TIGR02633 168 PSSSLtEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDtICVIRDGQHV 220
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
361-568 |
7.23e-11 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 62.64 E-value: 7.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 361 LNHVSLTFPAASMSA---------LVGASGAGKTTvtkLLMRYAD--PQQGQISIGGVDIRRLTP-----------EQLN 418
Cdd:PRK03695 3 LNDVAVSTRLGPLSAevrageilhLVGPNGAGKST---LLARMAGllPGSGSIQFAGQPLEAWSAaelarhraylsQQQT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 419 SLISV-VFQDVWLFDDTLlaniriARPQATRQEVEEAARAAQCLEFISRlpqgwltpmgeMGGQLSGGERQRISIARALL 497
Cdd:PRK03695 80 PPFAMpVFQYLTLHQPDK------TRTEAVASALNEVAEALGLDDKLGR-----------SVNQLSGGEWQRVRLAAVVL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 498 KNAPVV-------ILDEPTAALDIeselAVQKAIDNLVH-----NRTVIIIAHRLS-TIAGAGNILVIEEGQVVEQGTHA 564
Cdd:PRK03695 143 QVWPDInpagqllLLDEPMNSLDV----AQQAALDRLLSelcqqGIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRD 218
|
....
gi 1805558896 565 QLLS 568
Cdd:PRK03695 219 EVLT 222
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
482-539 |
8.01e-11 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 61.02 E-value: 8.01e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1805558896 482 LSGGERQRISIARALLKNAPVVILDEPTAALDIESELAVQKAIDNlvHNRTVIIIAHR 539
Cdd:cd03223 92 LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKE--LGITVISVGHR 147
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
355-582 |
9.11e-11 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 62.41 E-value: 9.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 355 EGDGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADP----QQGQISIGGVdirRLTPEQLNS-LISVVFQDVW 429
Cdd:PRK10418 13 QAAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGK---PVAPCALRGrKIATIMQNPR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 430 -LFD----------DTLLANIRIARPQATRQEVEEAAraaqcLEFISRLPQgwLTPMgemggQLSGGERQRISIARALLK 498
Cdd:PRK10418 90 sAFNplhtmhtharETCLALGKPADDATLTAALEAVG-----LENAARVLK--LYPF-----EMSGGMLQRMMIALALLC 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 499 NAPVVILDEPTAALDIESELAVQKAIDNLVHNRT--VIIIAHRLSTIAG-AGNILVIEEGQVVEQGTHAQLLS--HHGRY 573
Cdd:PRK10418 158 EAPFIIADEPTTDLDVVAQARILDLLESIVQKRAlgMLLVTHDMGVVARlADDVAVMSHGRIVEQGDVETLFNapKHAVT 237
|
....*....
gi 1805558896 574 QALWQAQMA 582
Cdd:PRK10418 238 RSLVSAHLA 246
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
365-540 |
1.15e-10 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 60.45 E-value: 1.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 365 SLTFPAASMSALVGASGAGKTTVtkllmryadpqqgqisiggvdirrltpeqLNSLISVVFQdvwlfddtllANIRIARP 444
Cdd:cd03227 15 DVTFGEGSLTIITGPNGSGKSTI-----------------------------LDAIGLALGG----------AQSATRRR 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 445 QATRQEVEEAARAAqclEFISRLPQgwltpmgemggqLSGGERQRISIARAL----LKNAPVVILDEPTAALDIESELAV 520
Cdd:cd03227 56 SGVKAGCIVAAVSA---ELIFTRLQ------------LSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQAL 120
|
170 180
....*....|....*....|.
gi 1805558896 521 QKAI-DNLVHNRTVIIIAHRL 540
Cdd:cd03227 121 AEAIlEHLVKGAQVIVITHLP 141
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
345-557 |
1.45e-10 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 63.69 E-value: 1.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 345 RFDNVSYRYEEGDghalnhvsltfpaasMSALVGASGAGKT-TVTKLLMRYADPQQGQISIGG--VDIRrlTPEQ-LNSL 420
Cdd:TIGR02633 275 RVDDVSFSLRRGE---------------ILGVAGLVGAGRTeLVQALFGAYPGKFEGNVFINGkpVDIR--NPAQaIRAG 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 421 ISVVFQDV----WLFDDTLLANIRIARPQ--ATRQEVEEAARAAQCLEFISRLPQGWLTPMGEMGGqLSGGERQRISIAR 494
Cdd:TIGR02633 338 IAMVPEDRkrhgIVPILGVGKNITLSVLKsfCFKMRIDAAAELQIIGSAIQRLKVKTASPFLPIGR-LSGGNQQKAVLAK 416
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1805558896 495 ALLKNAPVVILDEPTAALDIESELAVQKAIDNLVHNR-TVIIIAHRLSTIAG-AGNILVIEEGQV 557
Cdd:TIGR02633 417 MLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGvAIIVVSSELAEVLGlSDRVLVIGEGKL 481
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
347-576 |
1.53e-10 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 61.87 E-value: 1.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 347 DNVSYRYeeGDGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGG-----VDIRRLTPEQLNSLI 421
Cdd:PRK11701 10 RGLTKLY--GPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMrdgqlRDLYALSEAERRRLL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 422 ----SVVFQDVwlfDDTLL------ANI-------------RIaRPQATR--QEVE-EAARaaqclefISRLPqgwltpm 475
Cdd:PRK11701 88 rtewGFVHQHP---RDGLRmqvsagGNIgerlmavgarhygDI-RATAGDwlERVEiDAAR-------IDDLP------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 476 gemgGQLSGGERQRISIARALLKNAPVVILDEPTAALDIeselAVQKAIDNLVHNRT------VIIIAHRLStIAG--AG 547
Cdd:PRK11701 150 ----TTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDV----SVQARLLDLLRGLVrelglaVVIVTHDLA-VARllAH 220
|
250 260 270
....*....|....*....|....*....|.
gi 1805558896 548 NILVIEEGQVVEQGTHAQLLS--HHGRYQAL 576
Cdd:PRK11701 221 RLLVMKQGRVVESGLTDQVLDdpQHPYTQLL 251
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
359-561 |
1.57e-10 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 60.41 E-value: 1.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 359 HALNHVSLTFPAASMSALVGASGAGKTTVTkllmryadpQQGQISIGGVDIRRLTPeqlnslisvvfqdvwLFDDTLLan 438
Cdd:cd03238 9 HNLQNLDVSIPLNVLVVVTGVSGSGKSTLV---------NEGLYASGKARLISFLP---------------KFSRNKL-- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 439 IRIARpqatrqeveeaaraaqcLEFISRLPQGWLTPMGEMGgQLSGGERQRISIARALLKNAP--VVILDEPTAALDIES 516
Cdd:cd03238 63 IFIDQ-----------------LQFLIDVGLGYLTLGQKLS-TLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQD 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1805558896 517 ELAVQKAIDNLVH-NRTVIIIAHRLSTIAGAGNILVIEEGQ------VVEQG 561
Cdd:cd03238 125 INQLLEVIKGLIDlGNTVILIEHNLDVLSSADWIIDFGPGSgksggkVVFSG 176
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
343-566 |
1.89e-10 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 61.70 E-value: 1.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 343 DIRfdNVSYRyeEGDGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLTPEQLNSL-- 420
Cdd:PRK11831 9 DMR--GVSFT--RGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVrk 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 421 -ISVVFQDVWLFDD-TLLANirIARPqatrqeveeaaraaqcLEFISRLPQGWL--TPMGE------------MGGQLSG 484
Cdd:PRK11831 85 rMSMLFQSGALFTDmNVFDN--VAYP----------------LREHTQLPAPLLhsTVMMKleavglrgaaklMPSELSG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 485 GERQRISIARALLKNAPVVILDEPTAALDIESELAVQKAIDNLVH--NRTVIIIAHRLSTIAG-AGNILVIEEGQVVEQG 561
Cdd:PRK11831 147 GMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSalGVTCVVVSHDVPEVLSiADHAYIVADKKIVAHG 226
|
....*
gi 1805558896 562 THAQL 566
Cdd:PRK11831 227 SAQAL 231
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
54-321 |
2.00e-10 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349994 [Multi-domain] Cd Length: 294 Bit Score: 62.11 E-value: 2.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 54 IID-ALLRGDAPQLLNWAMAFSVAAIVTLVLrwyGLGFEYR-GHLAQA-THELRLRLGEQLRRVPLEKLQRGRAGEMNAL 130
Cdd:cd18550 25 IIDdALPQGDLGLLVLLALGMVAVAVASALL---GVVQTYLsARIGQGvMYDLRVQLYAHLQRMSLAFFTRTRTGEIQSR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 131 LLgsvdenlNYVIAIANIL---LLTIVTPLTASLATL----WIDWRLGLVMLLIFPLLVPFYYW----RRPAMRRQMQTL 199
Cdd:cd18550 102 LN-------NDVGGAQSVVtgtLTSVVSNVVTLVATLvamlALDWRLALLSLVLLPLFVLPTRRvgrrRRKLTREQQEKL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 200 GEahqrLSGDIVEF--AQGMMVLRTCGSDADKSRALLAHFNALENLQTRTHRQGAGATMLIASVVELGLQVVVLSGIVWV 277
Cdd:cd18550 175 AE----LNSIMQETlsVSGALLVKLFGREDDEAARFARRSRELRDLGVRQALAGRWFFAALGLFTAIGPALVYWVGGLLV 250
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1805558896 278 VTGTLNLAFLIAAVAMIMRFAEPMAMFISytSVVELIASA--LQRI 321
Cdd:cd18550 251 IGGGLTIGTLVAFTALLGRLYGPLTQLLN--IQVDLMTSLalFERI 294
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
350-590 |
2.47e-10 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 61.34 E-value: 2.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 350 SYRYEEGDGH-----ALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLTPEQLNSLISVV 424
Cdd:PRK15112 13 TFRYRTGWFRrqtveAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 425 FQDVwlfDDTLLANIRIAR----PQATRQEVEEAARAAQcleFISRLPQGWLTP--MGEMGGQLSGGERQRISIARALLK 498
Cdd:PRK15112 93 FQDP---STSLNPRQRISQildfPLRLNTDLEPEQREKQ---IIETLRQVGLLPdhASYYPHMLAPGQKQRLGLARALIL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 499 NAPVVILDEPTAALDieseLAVQKAIDNLV------HNRTVIIIAHRLSTIAG-AGNILVIEEGQVVEQGTHAQLL---- 567
Cdd:PRK15112 167 RPKVIIADEALASLD----MSMRSQLINLMlelqekQGISYIYVTQHLGMMKHiSDQVLVMHQGEVVERGSTADVLaspl 242
|
250 260 270
....*....|....*....|....*....|..
gi 1805558896 568 ---------SHHGryQALwqaqmAARVWRDDG 590
Cdd:PRK15112 243 heltkrliaGHFG--EAL-----TADAWRKDR 267
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
360-543 |
2.55e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 63.10 E-value: 2.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 360 ALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLTPEQLNSL-ISVVFQDVWLFDD-TLLA 437
Cdd:PRK10762 19 ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEAgIGIIHQELNLIPQlTIAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 438 NIRIARPQATR-------QEVEEAARAAQCLEfisrLPQGWLTPMGEmggqLSGGERQRISIARALLKNAPVVILDEPTA 510
Cdd:PRK10762 99 NIFLGREFVNRfgridwkKMYAEADKLLARLN----LRFSSDKLVGE----LSIGEQQMVEIAKVLSFESKVIIMDEPTD 170
|
170 180 190
....*....|....*....|....*....|....*
gi 1805558896 511 AL-DIESElAVQKAIDNL-VHNRTVIIIAHRLSTI 543
Cdd:PRK10762 171 ALtDTETE-SLFRVIRELkSQGRGIVYISHRLKEI 204
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
375-567 |
2.87e-10 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 60.63 E-value: 2.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 375 ALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLTPEqlnslISVVFQD---VWLFDDTLLANI------RIA--- 442
Cdd:TIGR03771 10 GLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGASPGKGWRH-----IGYVPQRhefAWDFPISVAHTVmsgrtgHIGwlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 443 RP-QATRQEVEEAARAAQCLEFISRlpqgwltPMGEmggqLSGGERQRISIARALLKNAPVVILDEPTAALDIES-ELAV 520
Cdd:TIGR03771 85 RPcVADFAAVRDALRRVGLTELADR-------PVGE----LSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTqELLT 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1805558896 521 QKAIDNLVHNRTVIIIAHRLSTIAGAGNILVIEEGQVVEQGTHAQLL 567
Cdd:TIGR03771 154 ELFIELAGAGTAILMTTHDLAQAMATCDRVVLLNGRVIADGTPQQLQ 200
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
356-561 |
3.07e-10 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 60.74 E-value: 3.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 356 GDGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMryADPQ----QGQISIGGVDIRRLTPEQLNSL-ISVVFQ---- 426
Cdd:TIGR01978 11 EDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIA--GHPSyevtSGTILFKGQDLLELEPDERARAgLFLAFQypee 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 427 ----DVWLFDDTLLANIRIARPQAT------RQEVEEA-ARAAQCLEFISR-LPQGWltpmgemggqlSGGERQRISIAR 494
Cdd:TIGR01978 89 ipgvSNLEFLRSALNARRSARGEEPldlldfEKLLKEKlALLDMDEEFLNRsVNEGF-----------SGGEKKRNEILQ 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 495 ALLKNAPVVILDEPTAALDIESELAVQKAIDNL-VHNRTVIIIAH--RLSTIAGAGNILVIEEGQVVEQG 561
Cdd:TIGR01978 158 MALLEPKLAILDEIDSGLDIDALKIVAEGINRLrEPDRSFLIITHyqRLLNYIKPDYVHVLLDGRIVKSG 227
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
344-513 |
3.15e-10 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 62.17 E-value: 3.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 344 IRFDNVSYRYEeGDGHALNHVSLTFPAASMSALVGASGAGKTTvtkLLMRYADPQQ---GQISIGGVDIRRLTPEQLNsl 420
Cdd:PRK11650 4 LKLQAVRKSYD-GKTQVIKGIDLDVADGEFIVLVGPSGCGKST---LLRMVAGLERitsGEIWIGGRVVNELEPADRD-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 421 ISVVFQDVWLFDD-TLLANI----RIAR-PQATRQE-VEEAARAAQCLEFISRLPQgwltpmgemggQLSGGERQRISIA 493
Cdd:PRK11650 78 IAMVFQNYALYPHmSVRENMayglKIRGmPKAEIEErVAEAARILELEPLLDRKPR-----------ELSGGQRQRVAMG 146
|
170 180
....*....|....*....|
gi 1805558896 494 RALLKNAPVVILDEPTAALD 513
Cdd:PRK11650 147 RAIVREPAVFLFDEPLSNLD 166
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
361-569 |
3.50e-10 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 60.43 E-value: 3.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 361 LNHVSLTFPAASMSALVGASGAGKTT----VTKLLMryadPQQGQISIGGVDI-----------------------RRLT 413
Cdd:COG1137 19 VKDVSLEVNQGEIVGLLGPNGAGKTTtfymIVGLVK----PDSGRIFLDGEDIthlpmhkrarlgigylpqeasifRKLT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 414 PEQlnslisvvfqdvwlfddtllaNIRIARPQATRQEVEEAARAAQCL-EF-ISRLpqgwltpMGEMGGQLSGGERQRIS 491
Cdd:COG1137 95 VED---------------------NILAVLELRKLSKKEREERLEELLeEFgITHL-------RKSKAYSLSGGERRRVE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 492 IARALLKNAPVVILDEPTAALDiesELAV---QKAIDNLV----------HN-RTVIIIAHRLStiagagnilVIEEGQV 557
Cdd:COG1137 147 IARALATNPKFILLDEPFAGVD---PIAVadiQKIIRHLKergigvlitdHNvRETLGICDRAY---------IISEGKV 214
|
250
....*....|..
gi 1805558896 558 VEQGTHAQLLSH 569
Cdd:COG1137 215 LAEGTPEEILNN 226
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
378-557 |
4.87e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 62.25 E-value: 4.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 378 GASGAGKT-TVTKLLMRYADPQQGQISIGG--VDIRrlTPEQ-LNSLISVVFQD------VWLFDdtLLANIRIARPQ-- 445
Cdd:PRK13549 295 GLVGAGRTeLVQCLFGAYPGRWEGEIFIDGkpVKIR--NPQQaIAQGIAMVPEDrkrdgiVPVMG--VGKNITLAALDrf 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 446 ATRQEVEEAARAAQCLEFISRLPQGWLTPMGEMGgQLSGGERQRISIARALLKNAPVVILDEPTAALDIESELAVQKAID 525
Cdd:PRK13549 371 TGGSRIDDAAELKTILESIQRLKVKTASPELAIA-RLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLIN 449
|
170 180 190
....*....|....*....|....*....|....
gi 1805558896 526 NLVHNR-TVIIIAHRLSTIAG-AGNILVIEEGQV 557
Cdd:PRK13549 450 QLVQQGvAIIVISSELPEVLGlSDRVLVMHEGKL 483
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
54-321 |
5.43e-10 |
|
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349987 [Multi-domain] Cd Length: 291 Bit Score: 60.57 E-value: 5.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 54 IID-ALLRGDAPQLLNWAMAFSVAAIVTLVL----RWYGlgfeyrGHLAQAT-HELRLRLGEQLRRVPLEKLQRGRAGEm 127
Cdd:cd18543 25 AIDgPIAHGDRSALWPLVLLLLALGVAEAVLsflrRYLA------GRLSLGVeHDLRTDLFAHLQRLDGAFHDRWQSGQ- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 128 nalLLGSVDENLNYVIAIANILLLTIVTPLTASLAT---LWIDWRLGLVMLLIFPLLVPF-YYWRR---PAMRRQMQTLG 200
Cdd:cd18543 98 ---LLSRATSDLSLVQRFLAFGPFLLGNLLTLVVGLvvmLVLSPPLALVALASLPPLVLVaRRFRRryfPASRRAQDQAG 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 201 EahqrLSGDIVEFAQGMMVLRTCGSDADKSRALLAHFNALENLQTRTHRQGAGATMLIASVVELGLQVVVLSGIVWVVTG 280
Cdd:cd18543 175 D----LATVVEESVTGIRVVKAFGRERRELDRFEAAARRLRATRLRAARLRARFWPLLEALPELGLAAVLALGGWLVANG 250
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1805558896 281 TLNLAFLIAAVAMIMRFAEPMAMFISYTSVVELIASALQRI 321
Cdd:cd18543 251 SLTLGTLVAFSAYLTMLVWPVRMLGWLLAMAQRARAAAERV 291
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
53-321 |
1.25e-09 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350008 [Multi-domain] Cd Length: 307 Bit Score: 59.83 E-value: 1.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 53 PIIDALLRGDAPQLLNWAmafsVAAIVTLVLRWYGLGF--EYRGHLA--QATHELRLRLGEQLRRVPLEKLQRGRAGEMN 128
Cdd:cd18564 39 LGLAPLLGPDPLALLLLA----AAALVGIALLRGLASYagTYLTALVgqRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 129 ALLLGSVDenlnyviAIANiLLLTIVTPLTASLATL--------WIDWRLGLVMLLIFPLLVPFYYWrrpaMRRQMQTLG 200
Cdd:cd18564 115 SRLTGDVG-------AIQD-LLVSGVLPLLTNLLTLvgmlgvmfWLDWQLALIALAVAPLLLLAARR----FSRRIKEAS 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 201 EAHQRLSGDIVEFAQ----GMMVLRTCGSDADKSRALLAHfnALENLQT--RTHRQGAGATMLIASVVELGLQVVVLSGI 274
Cdd:cd18564 183 REQRRREGALASVAQeslsAIRVVQAFGREEHEERRFARE--NRKSLRAglRAARLQALLSPVVDVLVAVGTALVLWFGA 260
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1805558896 275 VWVVTGTLNLAFLIAAVAMIMRFAEPMAMFISYTSVVELIASALQRI 321
Cdd:cd18564 261 WLVLAGRLTPGDLLVFLAYLKNLYKPVRDLAKLTGRIAKASASAERV 307
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
474-562 |
1.37e-09 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 59.17 E-value: 1.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 474 PMGEMGGQLSGGERQRISIARALLKNAP---VVILDEPTAAL---DIESELAVqkaIDNLVHN-RTVIIIAHRLSTIAGA 546
Cdd:cd03271 162 KLGQPATTLSGGEAQRIKLAKELSKRSTgktLYILDEPTTGLhfhDVKKLLEV---LQRLVDKgNTVVVIEHNLDVIKCA 238
|
90 100
....*....|....*....|..
gi 1805558896 547 GNILVI------EEGQVVEQGT 562
Cdd:cd03271 239 DWIIDLgpeggdGGGQVVASGT 260
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
481-541 |
1.39e-09 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 58.92 E-value: 1.39e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1805558896 481 QLSGGERQRISIARALLKNAPVVILDEPTAALDIESELAVQKAIDNLV-HNRTVIIIAHRLS 541
Cdd:cd03236 139 QLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAARLIRELAeDDNYVLVVEHDLA 200
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
357-513 |
1.63e-09 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 57.89 E-value: 1.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 357 DGHAL-NHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLTPEQLNSLisvvfqdVWL----- 430
Cdd:PRK13538 12 DERILfSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDL-------LYLghqpg 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 431 FDDTLLA--NIRIArpQATRQEV-EEAARAAqclefisrlpqgwLTPMGEMG------GQLSGGERQRISIARALLKNAP 501
Cdd:PRK13538 85 IKTELTAleNLRFY--QRLHGPGdDEALWEA-------------LAQVGLAGfedvpvRQLSAGQQRRVALARLWLTRAP 149
|
170
....*....|..
gi 1805558896 502 VVILDEPTAALD 513
Cdd:PRK13538 150 LWILDEPFTAID 161
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
34-301 |
2.01e-09 |
|
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349990 [Multi-domain] Cd Length: 292 Bit Score: 59.04 E-value: 2.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 34 MLALLLAAFMQGIAFACL--YPIIDALLRGDAPQLLNWAMAFSVAAIVTLVLRWygLGFEYRGHLAQA-THELRLRLGEQ 110
Cdd:cd18546 4 ALLLVVVDTAASLAGPLLvrYGIDSGVRAGDLGVLLLAAAAYLAVVLAGWVAQR--AQTRLTGRTGERlLYDLRLRVFAH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 111 LRRVPLEKLQRGRAGE-----------MNALLLGSVDEnlnyviAIANILLLTIVTpltasLATLWIDWRLGLVMLLIFP 179
Cdd:cd18546 82 LQRLSLDFHERETSGRimtrmtsdidaLSELLQTGLVQ------LVVSLLTLVGIA-----VVLLVLDPRLALVALAALP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 180 LLVPFYYWRRPAMRRQMQTLGEAHQRLSGDIVEFAQGMMVLRTCGSDADKSRALLAHFNALENLQTRTHRQGA---GATM 256
Cdd:cd18546 151 PLALATRWFRRRSSRAYRRARERIAAVNADLQETLAGIRVVQAFRRERRNAERFAELSDDYRDARLRAQRLVAiyfPGVE 230
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1805558896 257 LIAsvvELGLQVVVLSGIVWVVTGTLNLAFLIAAVAMIMRFAEPM 301
Cdd:cd18546 231 LLG---NLATAAVLLVGAWRVAAGTLTVGVLVAFLLYLRRFFAPI 272
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
344-558 |
2.26e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 60.13 E-value: 2.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 344 IRFDNVSYRYeeGDGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGG------VDIRR--LTPE 415
Cdd:PRK11819 325 IEAENLSKSF--GDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGEtvklayVDQSRdaLDPN 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 416 QlnslisVVFQDVWLFDDTllanIRIARpqatrqeVEEAARAaqcleFISRLpqgwltpmGEMG-------GQLSGGERQ 488
Cdd:PRK11819 403 K------TVWEEISGGLDI----IKVGN-------REIPSRA-----YVGRF--------NFKGgdqqkkvGVLSGGERN 452
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1805558896 489 RISIARALLKNAPVVILDEPTAALDIESELAVQKAIDNLVHnrTVIIIAH------RLSTiagagNILVIE-EGQVV 558
Cdd:PRK11819 453 RLHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALLEFPG--CAVVISHdrwfldRIAT-----HILAFEgDSQVE 522
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
375-546 |
2.63e-09 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 56.23 E-value: 2.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 375 ALVGASGAGKTTVTKLLMRYADPQQGQ-ISIGGVDIRRLTPEQLnslisvvfqdvwlfddtllaniriarpqatrqevee 453
Cdd:smart00382 6 LIVGPPGSGKTTLARALARELGPPGGGvIYIDGEDILEEVLDQL------------------------------------ 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 454 aaraaqclefisrlpqgWLTPMGEMGGQLSGGERQRISIARALLKNAPVVILDEPTAALDIESELAVQKAIDNLV----- 528
Cdd:smart00382 50 -----------------LLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLllllk 112
|
170 180
....*....|....*....|
gi 1805558896 529 --HNRTVIIIAHRLSTIAGA 546
Cdd:smart00382 113 seKNLTVILTTNDEKDLGPA 132
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
360-559 |
3.46e-09 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 59.42 E-value: 3.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 360 ALNHVSLTFPAASMSALVGASGAGKTTVTKLLM------RYadpqQGQISIGGV-----DIRrlTPEQLNslISVVFQDV 428
Cdd:NF040905 16 ALDDVNLSVREGEIHALCGENGAGKSTLMKVLSgvyphgSY----EGEILFDGEvcrfkDIR--DSEALG--IVIIHQEL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 429 WLFDDTLLA-NIRIARPQATRQEV---EEAARAAQCLEFI--SRLPQgwlTPMGEMGGqlsgGERQRISIARALLKNAPV 502
Cdd:NF040905 88 ALIPYLSIAeNIFLGNERAKRGVIdwnETNRRARELLAKVglDESPD---TLVTDIGV----GKQQLVEIAKALSKDVKL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1805558896 503 VILDEPTAAL-DIESElavqKAIDNLVHNR----TVIIIAHRLSTIAG-AGNILVIEEGQVVE 559
Cdd:NF040905 161 LILDEPTAALnEEDSA----ALLDLLLELKaqgiTSIIISHKLNEIRRvADSITVLRDGRTIE 219
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
92-321 |
4.76e-09 |
|
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar proteins; This group represents the homodimeric bacterial ABC multidrug exporter Sav1866, which is homologous to the lipid flippase MsbA, and both of which are functionally related to the human P-glycoprotein multidrug transporter (ABCB1 or MDR1). This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 349998 [Multi-domain] Cd Length: 299 Bit Score: 57.81 E-value: 4.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 92 YRGHLAQAT-----HELRLRLGEQLRRVPLEKLQRGRAGEMNALLLGSVDENLNYVIAIANILLLTIVTPLTASLATLWI 166
Cdd:cd18554 65 YRQYFAQWIankilYDIRKDLFDHLQKLSLRYYANNRSGEIISRVINDVEQTKDFITTGLMNIWLDMITIIIAICIMLVL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 167 DWRLGLVMLLIFP---LLVPFYYWR-RPAMRRQMQTLGEAHQRLSgdivEFAQGMMVLRTCGSDADKSRALLAHFNALEN 242
Cdd:cd18554 145 NPKLTFVSLVIFPfyiLAVKYFFGRlRKLTKERSQALAEVQGFLH----ERIQGMSVIKSFALEKHEQKQFDKRNGHFLT 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 243 LQTRTHRQGAGATMLIASVVELGLQVVVLSGIVWVVTGTLNLAFLIAAVAMIMRFAEPMAMFI-SYTSVVELIASaLQRI 321
Cdd:cd18554 221 RALKHTRWNAKTFSAVNTITDLAPLLVIGFAAYLVIEGNLTVGTLVAFVGYMERMYSPLRRLVnSFTTLTQSFAS-MDRV 299
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
348-539 |
5.40e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 56.50 E-value: 5.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 348 NVSYRYEegDGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLTPEQLNSLISVVFQD 427
Cdd:PRK13540 6 ELDFDYH--DQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFVGHRS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 428 VWLFDDTLLANIRI-ARPQATRQEVEEAARAAQcLEFISRLPQGWltpmgemggqLSGGERQRISIARALLKNAPVVILD 506
Cdd:PRK13540 84 GINPYLTLRENCLYdIHFSPGAVGITELCRLFS-LEHLIDYPCGL----------LSSGQKRQVALLRLWMSKAKLWLLD 152
|
170 180 190
....*....|....*....|....*....|....*..
gi 1805558896 507 EPTAALDiesELAVQKAIDNLVHNR----TVIIIAHR 539
Cdd:PRK13540 153 EPLVALD---ELSLLTIITKIQEHRakggAVLLTSHQ 186
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
34-321 |
8.25e-09 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349989 [Multi-domain] Cd Length: 293 Bit Score: 57.09 E-value: 8.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 34 MLALLLAAFMQGIAFACLYPI---ID-ALLRGDAPQLLNWAMAFSVAAIVTLVL---RWYglgfeYRGHLAQAT-HELRL 105
Cdd:cd18545 3 LLALLLMLLSTAASLAGPYLIkiaIDeYIPNGDLSGLLIIALLFLALNLVNWVAsrlRIY-----LMAKVGQRIlYDLRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 106 RLGEQLRRVPLEKLQRGRAGEMNALLLGSVDeNLNYVI------AIANILLLTIVTpltasLATLWIDWRLGLVMLLIFP 179
Cdd:cd18545 78 DLFSHLQKLSFSFFDSRPVGKILSRVINDVN-SLSDLLsnglinLIPDLLTLVGIV-----IIMFSLNVRLALVTLAVLP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 180 LLVPFYYWRRPAMRRQMQTLGEAHQRLSGDIVEFAQGMMVLRTCGSDADKSRallaHFNALENLQTRTHRQGAGATMLIA 259
Cdd:cd18545 152 LLVLVVFLLRRRARKAWQRVRKKISNLNAYLHESISGIRVIQSFAREDENEE----IFDELNRENRKANMRAVRLNALFW 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1805558896 260 SVVE----LGLQVVVLSGIVWVVTGTLNLAFLIAAVAMIMRFAEPMAMFIS-YTSVVELIASAlQRI 321
Cdd:cd18545 228 PLVElisaLGTALVYWYGGKLVLGGAITVGVLVAFIGYVGRFWQPIRNLSNfYNQLQSAMASA-ERI 293
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
344-561 |
1.24e-08 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 55.62 E-value: 1.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 344 IRFDNVSYRYEEGDG--------------------HALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQIS 403
Cdd:cd03220 1 IELENVSKSYPTYKGgssslkklgilgrkgevgefWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 404 IGGvdirrltpeqlnslisvvfQDVWL------FDDTLLA--NIRI-ARPQ-ATRQEVEEaaRAAQCLEFiSRLPQGWLT 473
Cdd:cd03220 81 VRG-------------------RVSSLlglgggFNPELTGreNIYLnGRLLgLSRKEIDE--KIDEIIEF-SELGDFIDL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 474 PMGEmggqLSGGERQRISIARALLKNAPVVILDEPTAALDIESELAVQKAIDNLV-HNRTVIIIAHRLSTIAGAGN-ILV 551
Cdd:cd03220 139 PVKT----YSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLkQGKTVILVSHDPSSIKRLCDrALV 214
|
250
....*....|
gi 1805558896 552 IEEGQVVEQG 561
Cdd:cd03220 215 LEKGKIRFDG 224
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
360-543 |
1.80e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 57.05 E-value: 1.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 360 ALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIR-RLTPEQLNSLISVVFQDVWLF-DDTLLA 437
Cdd:PRK10982 13 ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfKSSKEALENGISMVHQELNLVlQRSVMD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 438 NIRIARPQATRQEVEEAARAAQCLEFISRL-----PQgwltpmgEMGGQLSGGERQRISIARALLKNAPVVILDEPTAAL 512
Cdd:PRK10982 93 NMWLGRYPTKGMFVDQDKMYRDTKAIFDELdididPR-------AKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSL 165
|
170 180 190
....*....|....*....|....*....|...
gi 1805558896 513 DiESELAVQKAIDNLVHNR--TVIIIAHRLSTI 543
Cdd:PRK10982 166 T-EKEVNHLFTIIRKLKERgcGIVYISHKMEEI 197
|
|
| ABC_6TM_AarD_CydDC_like |
cd18561 |
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ... |
36-301 |
1.88e-08 |
|
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and similar proteins; The CydD protein, together with the CydC protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350005 [Multi-domain] Cd Length: 289 Bit Score: 56.13 E-value: 1.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 36 ALLLAAFMQGIafaclypiidaLLRGDAPQLLNWAMAFSVAAIVTLVLRWyglGFEYRGHLAQAT--HELRLRLGEQLRR 113
Cdd:cd18561 16 AWLLARALARI-----------FAGGPWEDIMPPLAGIAGVIVLRAALLW---LRERVAHRAAQRvkQHLRRRLFAKLLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 114 VPLEKLQRGRAGEMNALLLGSVDENLNYVIAIANILLLTIVTPLTASLATLWIDWRLG---LVMLLIFPLLVPFYYWRrp 190
Cdd:cd18561 82 LGPGYLEGERTGELQTTVVDGVEALEAYYGRYLPQLLVALLGPLLILIYLFFLDPLVAlilLVFALLIPLSPALWDRL-- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 191 aMRRQMQTLGEAHQRLSGDIVEFAQGMMVLRTCGSDADKSRALLAHFNALENLQTRTHRQGAGATMLIASVVELGLQVVV 270
Cdd:cd18561 160 -AKDTGRRHWAAYGRLSAQFLDSLQGMTTLKAFGASKRRGNELAARAEDLRQATMKVLAVSLLSSGIMGLATALGTALAL 238
|
250 260 270
....*....|....*....|....*....|.
gi 1805558896 271 LSGIVWVVTGTLNLAFLIAAVAMIMRFAEPM 301
Cdd:cd18561 239 GVGALRVLGGQLTLSSLLLILFLSREFFRPL 269
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
376-558 |
2.53e-08 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 56.57 E-value: 2.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 376 LVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLTPEQ-LNSLISVVFQD-----VWLfDDTLLANIRIA--RPQAT 447
Cdd:COG1129 283 IAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDaIRAGIAYVPEDrkgegLVL-DLSIRENITLAslDRLSR 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 448 RQEVEEAARAAQCLEFISRL---PQGWLTPMGemggQLSGGERQRISIARALLKNAPVVILDEPTAALDIESELAVQKAI 524
Cdd:COG1129 362 GGLLDRRRERALAEEYIKRLrikTPSPEQPVG----NLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLI 437
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1805558896 525 DNLVHN-RTVIII----------AHRlstiagagnILVIEEGQVV 558
Cdd:COG1129 438 RELAAEgKAVIVIsselpellglSDR---------ILVMREGRIV 473
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
366-517 |
3.54e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 54.11 E-value: 3.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 366 LTFPAASMSALV--GASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLTP-EQ---------LNSLISVVfqdvwlfdd 433
Cdd:PRK13539 21 LSFTLAAGEALVltGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVaEAchylghrnaMKPALTVA--------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 434 tllANIRI-ARPQATRQEVEEAARAAQCLEFISRLPqgwltpmgemGGQLSGGERQRISIARALLKNAPVVILDEPTAAL 512
Cdd:PRK13539 92 ---ENLEFwAAFLGGEELDIAAALEAVGLAPLAHLP----------FGYLSAGQKRRVALARLLVSNRPIWILDEPTAAL 158
|
....*
gi 1805558896 513 DIESE 517
Cdd:PRK13539 159 DAAAV 163
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
451-562 |
3.68e-08 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 56.56 E-value: 3.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 451 VEEAA-------RAAQCLEFISRLPQGWLtPMGEMGGQLSGGERQRISIARALLKNA---PVVILDEPTAAL---DIESE 517
Cdd:TIGR00630 793 VEEAYeffeavpSISRKLQTLCDVGLGYI-RLGQPATTLSGGEAQRIKLAKELSKRStgrTLYILDEPTTGLhfdDIKKL 871
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1805558896 518 LAVqkaIDNLVHN-RTVIIIAHRLSTIAGAGNILVI------EEGQVVEQGT 562
Cdd:TIGR00630 872 LEV---LQRLVDKgNTVVVIEHNLDVIKTADYIIDLgpeggdGGGTVVASGT 920
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
348-561 |
4.58e-08 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 53.81 E-value: 4.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 348 NVSYRYEEGDGHA--LNHVSLTFPAASMSALVGASGAGKTT----VTKLLMRYADPQqGQISIGGVDIRRlTPEQLNSLI 421
Cdd:cd03233 8 NISFTTGKGRSKIpiLKDFSGVVKPGEMVLVLGRPGSGCSTllkaLANRTEGNVSVE-GDIHYNGIPYKE-FAEKYPGEI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 422 SVVFQDVWLFddtllaniriarPQATrqeVEEAaraaqcLEFISRLpQGwltpmGEMGGQLSGGERQRISIARALLKNAP 501
Cdd:cd03233 86 IYVSEEDVHF------------PTLT---VRET------LDFALRC-KG-----NEFVRGISGGERKRVSIAEALVSRAS 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1805558896 502 VVILDEPTAALDIESELAVQKAIDNLVHnrtviiiAHRLSTIAG---AGN--------ILVIEEGQVVEQG 561
Cdd:cd03233 139 VLCWDNSTRGLDSSTALEILKCIRTMAD-------VLKTTTFVSlyqASDeiydlfdkVLVLYEGRQIYYG 202
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
375-538 |
6.43e-08 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 53.38 E-value: 6.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 375 ALVGASGAGKTTVTKLLmRYAdpqqgqisiggvdirrLTPEQLNSLISVVFQDvwlfddtllaniRIARPQATRQEVE-- 452
Cdd:cd03240 26 LIVGQNGAGKTTIIEAL-KYA----------------LTGELPPNSKGGAHDP------------KLIREGEVRAQVKla 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 453 ---------EAARAAQCLEFISRLPQG---WLTPmgEMGGQLSGGERQ------RISIARALLKNAPVVILDEPTAALDI 514
Cdd:cd03240 77 fenangkkyTITRSLAILENVIFCHQGesnWPLL--DMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDE 154
|
170 180
....*....|....*....|....*..
gi 1805558896 515 ES-ELAVQKAIDNLVH--NRTVIIIAH 538
Cdd:cd03240 155 ENiEESLAEIIEERKSqkNFQLIVITH 181
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
361-542 |
7.18e-08 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 53.02 E-value: 7.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 361 LNHVSLTFPAASMSALVGASGAGKTTVTKLLM--RYADPQQGQISIGGvdirRLTPEQLNSLISVVFQDvwlfdDTLLan 438
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLDVLAgrKTAGVITGEILING----RPLDKNFQRSTGYVEQQ-----DVHS-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 439 iriarPQATrqeVEEAaraaqcLEFiSRLPQGwltpmgemggqLSGGERQRISIARALLKNAPVVILDEPTAALDIESEL 518
Cdd:cd03232 92 -----PNLT---VREA------LRF-SALLRG-----------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAY 145
|
170 180
....*....|....*....|....*
gi 1805558896 519 AVQKAIDNLV-HNRTVIIIAHRLST 542
Cdd:cd03232 146 NIVRFLKKLAdSGQAILCTIHQPSA 170
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
361-571 |
8.08e-08 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 53.88 E-value: 8.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 361 LNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQ--QGQISIGGVDIRRLTPEQLNSL-ISVVFQdvWLFDDTLLA 437
Cdd:CHL00131 23 LKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAYKilEGDILFKGESILDLEPEERAHLgIFLAFQ--YPIEIPGVS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 438 NI---RIARPQATRQEVEEAARAAQCLEFISR------LPQGWLTPMGEMGgqLSGGERQRISIARALLKNAPVVILDEP 508
Cdd:CHL00131 101 NAdflRLAYNSKRKFQGLPELDPLEFLEIINEklklvgMDPSFLSRNVNEG--FSGGEKKRNEILQMALLDSELAILDET 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1805558896 509 TAALDIESELAVQKAIDNLVH-NRTVIIIAH--RLSTIAGAGNILVIEEGQVVEQG--THAQLLSHHG 571
Cdd:CHL00131 179 DSGLDIDALKIIAEGINKLMTsENSIILITHyqRLLDYIKPDYVHVMQNGKIIKTGdaELAKELEKKG 246
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
33-294 |
2.12e-07 |
|
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; The bacterial lipid flippase MsbA is found in Gram-negative bacteria and transports lipid A and lipopolysaccharide (LPS) from the cytoplasmic leaflet to the periplasmic leaflet of the inner membrane. MsbA is also a polyspecific transporter capable of transporting a broad spectrum of drug molecules. Additionally, MsbA exhibits significant sequence similarity to mammalian multidrug resistance (MDR) proteins such as human MDR protein 1 (MDR1) and LmrA from Lactococcus lactis. This subgroup also contains a putative transporter Brevibacillus brevis TycD; the location of the tycD gene within the Tyc (tyrocidine) biosynthesis operon suggests that TycD may play a role in the secretion of the cyclic decapeptide antibiotic tyrocidine. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349996 [Multi-domain] Cd Length: 292 Bit Score: 52.81 E-value: 2.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 33 SMLALLLAAFMQGIAFACLYPIIDALLRGDAPQLLNWaMAFSVAAIVTL----------VLRWYGLGfeyrghlaqATHE 102
Cdd:cd18552 4 AILGMILVAATTAALAWLLKPLLDDIFVEKDLEALLL-VPLAIIGLFLLrglasylqtyLMAYVGQR---------VVRD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 103 LRLRLGEQLRRVPLEKLQRGRAGEMNALLLGSVDENLNYVIAIANILL---LTIVTpLTASLatLWIDWRLGLVMLLIFP 179
Cdd:cd18552 74 LRNDLFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVrdpLTVIG-LLGVL--FYLDWKLTLIALVVLP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 180 LLV-PFYYWRRP---AMRRQMQTLGEAHQRLSgdivEFAQGMMVLRTCGSDADKSRALLAHFNALENLQTRTHRQGAGAT 255
Cdd:cd18552 151 LAAlPIRRIGKRlrkISRRSQESMGDLTSVLQ----ETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALSS 226
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1805558896 256 mliaSVVELgLQVVVLSGIVW-----VVTGTLN----LAFLIAAVAMI 294
Cdd:cd18552 227 ----PLMEL-LGAIAIALVLWyggyqVISGELTpgefISFITALLLLY 269
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
365-582 |
2.12e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 53.87 E-value: 2.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 365 SLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLTPEQLNSLISVVFQD------VWLFDDTLlan 438
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQKLVSDEWQRnntdmlSPGEDDTG--- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 439 iRIARpQATRQEVEEAARAAQCLEF--ISRLpqgwltpMGEMGGQLSGGERQRISIARALLKNAPVVILDEPTAALDIES 516
Cdd:PRK10938 100 -RTTA-EIIQDEVKDPARCEQLAQQfgITAL-------LDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVAS 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1805558896 517 ELAVQKAIDNLVHNR-TVIIIAHRLSTI-AGAGNILVIEEGQVVEQGTHAQLLShhgryQALWqAQMA 582
Cdd:PRK10938 171 RQQLAELLASLHQSGiTLVLVLNRFDEIpDFVQFAGVLADCTLAETGEREEILQ-----QALV-AQLA 232
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
480-573 |
3.91e-07 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 53.11 E-value: 3.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 480 GQ----LSGGERQRISIARALLKNAP---VVILDEPTAAL---DIESELAV-QKAIDNlvHNrTVIIIAHRLSTIAGAGN 548
Cdd:COG0178 821 GQpattLSGGEAQRVKLASELSKRSTgktLYILDEPTTGLhfhDIRKLLEVlHRLVDK--GN-TVVVIEHNLDVIKTADW 897
|
90 100 110
....*....|....*....|....*....|....*..
gi 1805558896 549 IlvIE---E-----GQVVEQGTHAQLL----SHHGRY 573
Cdd:COG0178 898 I--IDlgpEggdggGEIVAEGTPEEVAkvkaSYTGRY 932
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
348-543 |
5.29e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 52.80 E-value: 5.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 348 NVSY--RYEEGDGHALNHVSLTFPAASMSALVGASGAGKTTvtkLLMRYADPQQGQISIGG---VDIRRLTPEQLNSLIS 422
Cdd:TIGR00956 764 NLTYevKIKKEKRVILNNVDGWVKPGTLTALMGASGAGKTT---LLNVLAERVTTGVITGGdrlVNGRPLDSSFQRSIGY 840
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 423 VVFQDVWLFDDT----LLANIRIARPQA-TRQE----VEEAARAAQCLEFISRLpqgwltpMGEMGGQLSGGERQRISIA 493
Cdd:TIGR00956 841 VQQQDLHLPTSTvresLRFSAYLRQPKSvSKSEkmeyVEEVIKLLEMESYADAV-------VGVPGEGLNVEQRKRLTIG 913
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1805558896 494 RALL-KNAPVVILDEPTAALDIESELAVQKAIDNLV-HNRTVIIIAHRLSTI 543
Cdd:TIGR00956 914 VELVaKPKLLLFLDEPTSGLDSQTAWSICKLMRKLAdHGQAILCTIHQPSAI 965
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
54-321 |
7.49e-07 |
|
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar proteins; This group represents the six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA from Lactococcus lactis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349995 [Multi-domain] Cd Length: 289 Bit Score: 51.28 E-value: 7.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 54 IIDALLRGDApqLLNWAMAFSVAAIVTLVLRWYGL-GFEYRGHlaQATHELRLRLGEQLRRVPLEKLQRGRAGEMnALLL 132
Cdd:cd18551 25 LIDALSAGGS--SGGLLALLVALFLLQAVLSALSSyLLGRTGE--RVVLDLRRRLWRRLLRLPVSFFDRRRSGDL-VSRV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 133 GSVDENLNYVIAIANILLLTIVTPLTASLATL-WIDWRLGLVMLLIFPLLVPFYYwrrPAMRRqMQTLGEAHQ----RLS 207
Cdd:cd18551 100 TNDTTLLRELITSGLPQLVTGVLTVVGAVVLMfLLDWVLTLVTLAVVPLAFLIIL---PLGRR-IRKASKRAQdalgELS 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 208 GDIVEFAQGMMVLRTCGSDADKSRALLAHFNALENLQTRTHRQGAGATMLIASVVELGLQVVVLSGIVWVVTGTLNLAFL 287
Cdd:cd18551 176 AALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALIGPLMGLAVQLALLVVLGVGGARVASGALTVGTL 255
|
250 260 270
....*....|....*....|....*....|....*
gi 1805558896 288 IAAVAMIMRFAEPMAMFIS-YTSVVELIAsALQRI 321
Cdd:cd18551 256 VAFLLYLFQLITPLSQLSSfFTQLQKALG-ALERI 289
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
375-569 |
7.92e-07 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 52.19 E-value: 7.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 375 ALVGASGAGKTTvtkLLMRYADPQQGQISIGGVDI--RRLTpEQLNSLISVVFQDVWLFD-----DTLLANIRIARPQA- 446
Cdd:PLN03211 98 AVLGPSGSGKST---LLNALAGRIQGNNFTGTILAnnRKPT-KQILKRTGFVTQDDILYPhltvrETLVFCSLLRLPKSl 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 447 TRQEVEEAARAAqclefISRLPqgwLTPMGE--MGGQ----LSGGERQRISIARALLKNAPVVILDEPTAALDIESELAV 520
Cdd:PLN03211 174 TKQEKILVAESV-----ISELG---LTKCENtiIGNSfirgISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRL 245
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1805558896 521 QKAIDNLVHN-RTVIIIAHRLST--IAGAGNILVIEEGQVVEQGTHAQLLSH 569
Cdd:PLN03211 246 VLTLGSLAQKgKTIVTSMHQPSSrvYQMFDSVLVLSEGRCLFFGKGSDAMAY 297
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
316-524 |
8.78e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 52.09 E-value: 8.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 316 SALQRIERFMAIAPL----PVAEQSEMPERYD---IRFDNVSYRYeeGDGHALNHVSLTFPAASMSALVGASGAGKTTVT 388
Cdd:PRK10636 278 SRIKMLERMELIAPAhvdnPFHFSFRAPESLPnplLKMEKVSAGY--GDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLI 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 389 KLLMRYADPQQGQISIG-GVDIRRLTPEQLNSLISvvfqdvwlfDDTLLANI-RIArPQATRQEVEEaaraaqclefisr 466
Cdd:PRK10636 356 KLLAGELAPVSGEIGLAkGIKLGYFAQHQLEFLRA---------DESPLQHLaRLA-PQELEQKLRD------------- 412
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1805558896 467 lpqgWLTPMG-------EMGGQLSGGERQRISIARALLKNAPVVILDEPTAALDIESELAVQKAI 524
Cdd:PRK10636 413 ----YLGGFGfqgdkvtEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEAL 473
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
473-567 |
1.05e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 51.54 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 473 TP-MGEMGGQLSGGERQRISIARALLKNAPVVILDEPTAALDIeselAVQKAIDNLVhNR------TVIIIAHRLSTIAG 545
Cdd:PRK10762 386 TPsMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDV----GAKKEIYQLI-NQfkaeglSIILVSSEMPEVLG 460
|
90 100
....*....|....*....|....*...
gi 1805558896 546 AGN-ILVIEEGQV-----VEQGTHAQLL 567
Cdd:PRK10762 461 MSDrILVMHEGRIsgeftREQATQEKLM 488
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
346-541 |
1.36e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 51.77 E-value: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 346 FDNVSY-------RYEEGDG----HALNHVSLTFPAASMSALVGASGAGKTTVTKLLM--RYADPQQGQISIGGVDIRRL 412
Cdd:PLN03140 870 FDDVNYfvdmpaeMKEQGVTedrlQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAgrKTGGYIEGDIRISGFPKKQE 949
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 413 T-------PEQlNSLIS--VVFQDVWLFDDTLLANIRIARPQATR--QEVEEAARAAQCLEFISRLPqgwltpmGEMGgq 481
Cdd:PLN03140 950 TfarisgyCEQ-NDIHSpqVTVRESLIYSAFLRLPKEVSKEEKMMfvDEVMELVELDNLKDAIVGLP-------GVTG-- 1019
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1805558896 482 LSGGERQRISIARALLKNAPVVILDEPTAALDIESELAVQKAIDNLVHN-RTVIIIAHRLS 541
Cdd:PLN03140 1020 LSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTgRTVVCTIHQPS 1080
|
|
| ABC_6TM_CydC |
cd18585 |
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH ... |
100-336 |
1.81e-06 |
|
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH transporter; The CydC protein, together with the CydD protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350029 [Multi-domain] Cd Length: 290 Bit Score: 49.79 E-value: 1.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 100 THELRLRLGEQLRR------VPL--EKLQRGRAGEMNALLLGSVD--ENLnYVIAIANILLLTIVTPLTaSLATLWIDWR 169
Cdd:cd18585 59 SHDATFRLLSNLRVwfyrklEPLapARLQKYRSGDLLNRIVADIDtlDNL-YLRVLSPPVVALLVILAT-ILFLAFFSPA 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 170 LGLVMLLIFPL---LVP--FYYWRRPAMRRQMQTLGEahqrLSGDIVEFAQGMMVLRTCGSDADKSRALLAHFNALENLQ 244
Cdd:cd18585 137 LALILLAGLLLagvVIPllFYRLGKKIGQQLVQLRAE----LRTELVDGLQGMAELLIFGALERQRQQLEQLSDALIKEQ 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 245 TRTHRQGAGATMLIASVVELGLQVVVLSGIVWVVTGTLNLAFLiaavamimrfaePMAMFISYTSvveliasalqrierF 324
Cdd:cd18585 213 RRLARLSGLSQALMILLSGLTVWLVLWLGAPLVQNGALDGALL------------AMLVFAVLAS--------------F 266
|
250
....*....|..
gi 1805558896 325 MAIAPLPVAEQS 336
Cdd:cd18585 267 EAVAPLPLAFQY 278
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
53-304 |
2.00e-06 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350009 [Multi-domain] Cd Length: 313 Bit Score: 49.87 E-value: 2.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 53 PIIDALLRGDAPQLLNWAMAFSVAA-IVTLVLRW-YGLGFeyrGHLAQAT-HELRLRLGEQLRRVPLEKLQRGRAGEMNA 129
Cdd:cd18565 39 LVPASLGPADPRGQLWLLGGLTVAAfLLESLFQYlSGVLW---RRFAQRVqHDLRTDTYDHVQRLDMAFFEDRQTGDLMS 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 130 LLLGSVDeNLNYVI-AIANILLLTIVTPLTASLATLWIDWRLGLVMLLIFPLLVPFYYW--RR--PAMRRQMQTLGEAHQ 204
Cdd:cd18565 116 VLNNDVN-QLERFLdDGANSIIRVVVTVLGIGAILFYLNWQLALVALLPVPLIIAGTYWfqRRiePRYRAVREAVGDLNA 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 205 RLSGDIvefaQGMMVLRTCGSDADKSRALLAHFNALENLQTRTHRQGAGATMLIASVVELGLQVVVLSGIVWVV------ 278
Cdd:cd18565 195 RLENNL----SGIAVIKAFTAEDFERERVADASEEYRDANWRAIRLRAAFFPVIRLVAGAGFVATFVVGGYWVLdgpplf 270
|
250 260
....*....|....*....|....*.
gi 1805558896 279 TGTLNLAFLIAAVAMIMRFAEPMAMF 304
Cdd:cd18565 271 TGTLTVGTLVTFLFYTQRLLWPLTRL 296
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
344-562 |
2.83e-06 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 48.92 E-value: 2.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 344 IRFDNVSYRYEEGDG--------------------HALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQIS 403
Cdd:COG1134 5 IEVENVSKSYRLYHEpsrslkelllrrrrtrreefWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 404 IGGvdirRLTPeqlnsLISV--VFQDvwlfDDTLLANIR-IARPQ-ATRQEVEEAARA----AQCLEFISrlpqgwlTPM 475
Cdd:COG1134 85 VNG----RVSA-----LLELgaGFHP----ELTGRENIYlNGRLLgLSRKEIDEKFDEivefAELGDFID-------QPV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 476 gemgGQLSGGERQRISIARALLKNAPVVILDEPTAALDIESELAVQKAIDNLV-HNRTVIIIAHRLSTIAG-AGNILVIE 553
Cdd:COG1134 145 ----KTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELReSGRTVIFVSHSMGAVRRlCDRAIWLE 220
|
....*....
gi 1805558896 554 EGQVVEQGT 562
Cdd:COG1134 221 KGRLVMDGD 229
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
480-573 |
2.86e-06 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 50.46 E-value: 2.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 480 GQ----LSGGERQRISIARALLKNA---PVVILDEPTAAL---DIESELAV-QKAIDNlvhNRTVIIIAHRLSTI----- 543
Cdd:PRK00349 825 GQpattLSGGEAQRVKLAKELSKRStgkTLYILDEPTTGLhfeDIRKLLEVlHRLVDK---GNTVVVIEHNLDVIktadw 901
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1805558896 544 -------AGAGNilvieeGQVVEQGTHAQLL----SHHGRY 573
Cdd:PRK00349 902 iidlgpeGGDGG------GEIVATGTPEEVAkveaSYTGRY 936
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
347-552 |
3.53e-06 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 49.64 E-value: 3.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 347 DNVSYRYEEGdGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLTPEQLNSL-ISVVF 425
Cdd:COG3845 261 ENLSVRDDRG-VPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLgVAYIP 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 426 QD-----------VWlfDDTLLANIRiARPQATRQEVEEAARAAQCLEFISRL---PQGWLTPMGemggQLSGGERQRIS 491
Cdd:COG3845 340 EDrlgrglvpdmsVA--ENLILGRYR-RPPFSRGGFLDRKAIRAFAEELIEEFdvrTPGPDTPAR----SLSGGNQQKVI 412
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1805558896 492 IARALLKNAPVVILDEPTAALDIeselavqKAIdNLVHNRtviIIAHRlstIAGAGnILVI 552
Cdd:COG3845 413 LARELSRDPKLLIAAQPTRGLDV-------GAI-EFIHQR---LLELR---DAGAA-VLLI 458
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
361-564 |
3.77e-06 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 48.63 E-value: 3.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 361 LNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQ--QGQISIGGVDIRRLTPEQ-LNSLISVVFQ--------DVW 429
Cdd:PRK09580 17 LRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYEvtGGTVEFKGKDLLELSPEDrAGEGIFMAFQypveipgvSNQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 430 LFDDTLLANIRIARPQATRQEVEEAARAAQCLEFIsRLPQGWLTPMGEMGgqLSGGERQRISIARALLKNAPVVILDEPT 509
Cdd:PRK09580 97 FFLQTALNAVRSYRGQEPLDRFDFQDLMEEKIALL-KMPEDLLTRSVNVG--FSGGEKKRNDILQMAVLEPELCILDESD 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1805558896 510 AALDIESELAVQKAIDNLVH-NRTVIIIAH--RLSTIAGAGNILVIEEGQVVEQGTHA 564
Cdd:PRK09580 174 SGLDIDALKIVADGVNSLRDgKRSFIIVTHyqRILDYIKPDYVHVLYQGRIVKSGDFT 231
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
356-538 |
3.86e-06 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 49.93 E-value: 3.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 356 GDGHALNHVSLTF-PAASMsALVGASGAGKTTVTKLlMRYAD--------PQQGqISIG--------------------G 406
Cdd:TIGR03719 16 PKKEILKDISLSFfPGAKI-GVLGLNGAGKSTLLRI-MAGVDkdfngearPQPG-IKVGylpqepqldptktvrenveeG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 407 V-DIRRLTPEqLNSlISVVFQDVWLFDDTLLANiriarpQATRQEVEEAA----------RAAQCLefisRLPQgWLTPM 475
Cdd:TIGR03719 93 VaEIKDALDR-FNE-ISAKYAEPDADFDKLAAE------QAELQEIIDAAdawdldsqleIAMDAL----RCPP-WDADV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1805558896 476 GEmggqLSGGERQRISIARALLKNAPVVILDEPTAALDIESELAVQKAIDNlvHNRTVIIIAH 538
Cdd:TIGR03719 160 TK----LSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQE--YPGTVVAVTH 216
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
344-513 |
5.76e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 49.35 E-value: 5.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 344 IRFDNVSYRYeeGDGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDI------RRLTPeql 417
Cdd:NF033858 2 ARLEGVSHRY--GKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMadarhrRAVCP--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 418 nslisvvfqdvwlfddtllaniRIA-RPQ-------AT---RQEVEEAAR-----AAQCLEFISRLPQ--GwLTPMGEM- 478
Cdd:NF033858 77 ----------------------RIAyMPQglgknlyPTlsvFENLDFFGRlfgqdAAERRRRIDELLRatG-LAPFADRp 133
|
170 180 190
....*....|....*....|....*....|....*
gi 1805558896 479 GGQLSGGERQRISIARALLKNAPVVILDEPTAALD 513
Cdd:NF033858 134 AGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVD 168
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
375-540 |
5.79e-06 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 49.63 E-value: 5.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 375 ALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIrrLTPeqlnslISVVFQDVWL---FD--DTLLANIR----IARPQ 445
Cdd:TIGR01257 1969 GLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI--LTN------ISDVHQNMGYcpqFDaiDDLLTGREhlylYARLR 2040
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 446 AT-RQEVEEAARAAqclefISRLpqGWLTPMGEMGGQLSGGERQRISIARALLKNAPVVILDEPTAALDIESELAVQKAI 524
Cdd:TIGR01257 2041 GVpAEEIEKVANWS-----IQSL--GLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTI 2113
|
170
....*....|....*..
gi 1805558896 525 DNLV-HNRTVIIIAHRL 540
Cdd:TIGR01257 2114 VSIIrEGRAVVLTSHSM 2130
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
35-321 |
5.93e-06 |
|
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349985 [Multi-domain] Cd Length: 293 Bit Score: 48.18 E-value: 5.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 35 LALLLAAFMQgiafacLYP------IIDALLRG--DAPQLLNWAMAFSVAAIVTLVLRWYglgfeYRGHLAQA----THE 102
Cdd:cd18541 6 LFLILVDLLQ------LLIpriigrAIDALTAGtlTASQLLRYALLILLLALLIGIFRFL-----WRYLIFGAsrriEYD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 103 LRLRLGEQLRRVPLEKLQRGRAGEMNALL---LGSVDENLNY-VIAIANILLLTIVTPLtaslATLWIDWRLGLVMLLIF 178
Cdd:cd18541 75 LRNDLFAHLLTLSPSFYQKNRTGDLMARAtndLNAVRMALGPgILYLVDALFLGVLVLV----MMFTISPKLTLIALLPL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 179 PLLVPFYYWRRPAMRRQMQTLGEAHQRLSGDIVEFAQGMMVLRTCGSD-------ADKSRALLAHFNALENLQtrthrqg 251
Cdd:cd18541 151 PLLALLVYRLGKKIHKRFRKVQEAFSDLSDRVQESFSGIRVIKAFVQEeaeierfDKLNEEYVEKNLRLARVD------- 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1805558896 252 agATM--LIASVVELGLQVVVLSGIVWVVTGTLNLAFLIAAVAMIMRFAEPMAMFISYTSVVELIASALQRI 321
Cdd:cd18541 224 --ALFfpLIGLLIGLSFLIVLWYGGRLVIRGTITLGDLVAFNSYLGMLIWPMMALGWVINLIQRGAASLKRI 293
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
480-557 |
1.03e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 48.19 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 480 GQLSGGERQRISIARALLKNAPVVILDEPTAALDIESELAVQKAIDNLVH-NRTVIIIAHRLSTIAGAGN-ILVIEEGQV 557
Cdd:PRK10982 390 GSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKkDKGIIIISSEMPELLGITDrILVMSNGLV 469
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
378-515 |
2.21e-05 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 46.00 E-value: 2.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 378 GASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLTPEQLNSLIS---VVFQDVWLFDDT-LLANIRIARPQatrqevee 453
Cdd:PRK13543 44 GDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRFMAYLGhlpGLKADLSTLENLhFLCGLHGRRAK-------- 115
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1805558896 454 aaraaqclefisRLPQGWLTPMGEMG------GQLSGGERQRISIARALLKNAPVVILDEPTAALDIE 515
Cdd:PRK13543 116 ------------QMPGSALAIVGLAGyedtlvRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLE 171
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
342-573 |
2.36e-05 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 47.19 E-value: 2.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 342 YDIRFDNVSYRYE---------------EGDG---HALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQIS 403
Cdd:PRK13545 3 YKVKFEHVTKKYKmynkpfdklkdlffrSKDGeyhYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 404 IGGVDIRRLTPEQLNSLIsvvfqdvwlfddTLLANIRIARPQA--TRQEVEEAarAAQCLEFisrlpqgwlTPMGEMGGQ 481
Cdd:PRK13545 83 IKGSAALIAISSGLNGQL------------TGIENIELKGLMMglTKEKIKEI--IPEIIEF---------ADIGKFIYQ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 482 ----LSGGERQRISIARALLKNAPVVILDEptaALDIESELAVQKAIDNL----VHNRTVIIIAHRLSTIAG-AGNILVI 552
Cdd:PRK13545 140 pvktYSSGMKSRLGFAISVHINPDILVIDE---ALSVGDQTFTKKCLDKMnefkEQGKTIFFISHSLSQVKSfCTKALWL 216
|
250 260
....*....|....*....|.
gi 1805558896 553 EEGQVVEQGTHAQLLSHHGRY 573
Cdd:PRK13545 217 HYGQVKEYGDIKEVVDHYDEF 237
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
452-569 |
2.75e-05 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 47.32 E-value: 2.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 452 EEAARAAQCL-EFISRLP------QGWLTPmGEMGGQLSGGERQRISIARALLKNAPVV--ILDEPTAAL---DIEsela 519
Cdd:TIGR00630 453 EEKKIAEEVLkEIRERLGflidvgLDYLSL-SRAAGTLSGGEAQRIRLATQIGSGLTGVlyVLDEPSIGLhqrDNR---- 527
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1805558896 520 vqKAIDNLVHNR----TVIIIAHRLSTIA----------GAGnilvIEEGQVVEQGTHAQLLSH 569
Cdd:TIGR00630 528 --RLINTLKRLRdlgnTLIVVEHDEDTIRaadyvidigpGAG----EHGGEVVASGTPEEILAN 585
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
358-568 |
2.87e-05 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 46.83 E-value: 2.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 358 GHALNH-VSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGG--VDIRR----------LTPEQLNS----- 419
Cdd:PRK11288 265 GPGLREpISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGkpIDIRSprdairagimLCPEDRKAegiip 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 420 LISVvfQDvwlfddtllaNIRI-ARPQATR--------QEVEEAARaaqcleFISRLPQGwlTPMGEMG-GQLSGGERQR 489
Cdd:PRK11288 345 VHSV--AD----------NINIsARRHHLRagclinnrWEAENADR------FIRSLNIK--TPSREQLiMNLSGGNQQK 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 490 ISIARALLKNAPVVILDEPTAALDI--ESElavqkaIDNLVHN-----RTVIIIAHRLSTIAG-AGNILVIEEGQVV--- 558
Cdd:PRK11288 405 AILGRWLSEDMKVILLDEPTRGIDVgaKHE------IYNVIYElaaqgVAVLFVSSDLPEVLGvADRIVVMREGRIAgel 478
|
250
....*....|..
gi 1805558896 559 --EQGTHAQLLS 568
Cdd:PRK11288 479 arEQATERQALS 490
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
359-561 |
3.05e-05 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 45.71 E-value: 3.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 359 HALNHVSLTFPAASMSALVGASGAGKTT--------------VTKLLMrYADPQQGQISIGGVD-IRRLTPEqlnslISV 423
Cdd:cd03270 9 HNLKNVDVDIPRNKLVVITGVSGSGKSSlafdtiyaegqrryVESLSA-YARQFLGQMDKPDVDsIEGLSPA-----IAI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 424 vfqdvwlfDDTLLANiriaRPQATRQEVEEA--------ARAA--QCLEFISRLPQGWLTpMGEMGGQLSGGERQRISIA 493
Cdd:cd03270 83 --------DQKTTSR----NPRSTVGTVTEIydylrllfARVGirERLGFLVDVGLGYLT-LSRSAPTLSGGEAQRIRLA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 494 RALLKNAPVV--ILDEPTAAL---DIeselavQKAIDNLVHNR----TVIIIAHRLSTIAGAGNILVI------EEGQVV 558
Cdd:cd03270 150 TQIGSGLTGVlyVLDEPSIGLhprDN------DRLIETLKRLRdlgnTVLVVEHDEDTIRAADHVIDIgpgagvHGGEIV 223
|
...
gi 1805558896 559 EQG 561
Cdd:cd03270 224 AQG 226
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
144-306 |
3.91e-05 |
|
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette transporters; This group includes the 6-TMD of the peptidase-containing ATP-binding cassette transporters (PCATs) such as Clostridium thermocellum PCAT1, a polypeptide processing and secretion transporter, and LagD, a bacteriocin ABC transporter from Lactococcus lactis. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs. The transporters involved in protein secretion often contain additional peptidase domains essential for substrate processing. These peptidase domains belong to the cysteine protease superfamily, classified as family C39, bacteriocin-processing peptidase. LagD is highly similar to the peptidase-containing ATP-binding cassette transporters (PCATs). In Gram-positive bacteria, the PCATs are responsible for exporting quorum-sensing or antimicrobial peptides called bacteriocins.
Pssm-ID: 350014 [Multi-domain] Cd Length: 294 Bit Score: 45.90 E-value: 3.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 144 AIANILLLTIVTPLTA--SLATL-WIDWRLGLVMLLIFPLLVPFYYWRRPAMRRQMQTLGEAHQRLSGDIVEFAQGMMVL 220
Cdd:cd18570 114 AISSTTISLFLDLLMViiSGIILfFYNWKLFLITLLIIPLYILIILLFNKPFKKKNREVMESNAELNSYLIESLKGIETI 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 221 RTCGSDADKSRALLAHFNALENLQTRTHR----QGAgatmlIASVVELGLQVVVLS-GIVWVVTGTLNLAFLIAAVAMIM 295
Cdd:cd18570 194 KSLNAEEQFLKKIEKKFSKLLKKSFKLGKlsnlQSS-----IKGLISLIGSLLILWiGSYLVIKGQLSLGQLIAFNALLG 268
|
170
....*....|.
gi 1805558896 296 RFAEPMAMFIS 306
Cdd:cd18570 269 YFLGPIENLIN 279
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
482-573 |
4.58e-05 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 46.56 E-value: 4.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 482 LSGGERQRISIARAL---LKNapVV-ILDEPTAAL---DIEselavqKAIDNLVHNR----TVIIIAHRLSTIA------ 544
Cdd:COG0178 486 LSGGEAQRIRLATQIgsgLVG--VLyVLDEPSIGLhqrDND------RLIETLKRLRdlgnTVIVVEHDEDTIRaadyii 557
|
90 100 110
....*....|....*....|....*....|....*..
gi 1805558896 545 ----GAGnilvIEEGQVVEQGTHAQLLSHH----GRY 573
Cdd:COG0178 558 digpGAG----EHGGEVVAQGTPEEILKNPdsltGQY 590
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
361-568 |
4.89e-05 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 45.59 E-value: 4.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 361 LNHVSLTFPAASMSALVGASGAGKTTvtkLLMRYADPQQGQISIGGVDIR---RLTPEQLNSLisvvfqdvwlfDDTLLA 437
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKST---LLKALAGDLTGGGAPRGARVTgdvTLNGEPLAAI-----------DAPRLA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 438 NIRIARPQATRQEVEEAARAaqcLEFISRLPQ----------------------GWLTPMGEMGGQLSGGERQRISIARA 495
Cdd:PRK13547 83 RLRAVLPQAAQPAFAFSARE---IVLLGRYPHarragalthrdgeiawqalalaGATALVGRDVTTLSGGELARVQFARV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 496 LLKNAP---------VVILDEPTAALDIESELAVQKAIDNLVH--NRTVIIIAHRLSTIA-GAGNILVIEEGQVVEQGTH 563
Cdd:PRK13547 160 LAQLWPphdaaqpprYLLLDEPTAALDLAHQHRLLDTVRRLARdwNLGVLAIVHDPNLAArHADRIAMLADGAIVAHGAP 239
|
....*
gi 1805558896 564 AQLLS 568
Cdd:PRK13547 240 ADVLT 244
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
54-304 |
5.13e-05 |
|
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (TrmA) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349988 [Multi-domain] Cd Length: 294 Bit Score: 45.46 E-value: 5.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 54 IIDALL---RGDAPQLLNWAMAFSVAAIVTLVLRWYglgFEYR-GHLAQ-ATHELRLRLGEQLRRVPLEKLQRGRAGEMN 128
Cdd:cd18544 25 AIDDYIvpgQGDLQGLLLLALLYLGLLLLSFLLQYL---QTYLlQKLGQrIIYDLRRDLFSHIQRLPLSFFDRTPVGRLV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 129 ALLLGSVdENLN--YVIAIANIL--LLTIVTPLTASLatlWIDWRLGLVMLLIFPLLVPFYYWRRPAMRRQMQTLGEAHQ 204
Cdd:cd18544 102 TRVTNDT-EALNelFTSGLVTLIgdLLLLIGILIAMF---LLNWRLALISLLVLPLLLLATYLFRKKSRKAYREVREKLS 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 205 RLSGDIVEFAQGMMVLRTCGsdadKSRALLAHFNALenlqTRTHRQGAGATMLIASV----VELgLQVVVLSGIVW---- 276
Cdd:cd18544 178 RLNAFLQESISGMSVIQLFN----REKREFEEFDEI----NQEYRKANLKSIKLFALfrplVEL-LSSLALALVLWyggg 248
|
250 260
....*....|....*....|....*....
gi 1805558896 277 -VVTGTLNLAFLIAAVAMIMRFAEPMAMF 304
Cdd:cd18544 249 qVLSGAVTLGVLYAFIQYIQRFFRPIRDL 277
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
480-516 |
6.05e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 45.88 E-value: 6.05e-05
10 20 30
....*....|....*....|....*....|....*..
gi 1805558896 480 GQLSGGERQRISIARALLKNAPVVILDEPTAALDIES 516
Cdd:PRK11819 162 TKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES 198
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
343-538 |
6.94e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 46.01 E-value: 6.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 343 DIRFDNVSYRYeeGDGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYAD---PQQGQI-----SIGGVDIRRLT- 413
Cdd:PLN03073 177 DIHMENFSISV--GGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMAMHAIdgiPKNCQIlhveqEVVGDDTTALQc 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 414 --------PEQLNSLISVVFQDVWLFDDTLLANIRIA-----RPQATRQEVEE-------------AARAAQCLEFISRL 467
Cdd:PLN03073 255 vlntdierTQLLEEEAQLVAQQRELEFETETGKGKGAnkdgvDKDAVSQRLEEiykrlelidaytaEARAASILAGLSFT 334
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1805558896 468 PQGWLtpmgEMGGQLSGGERQRISIARALLKNAPVVILDEPTAALDIESELAVQKAIdnLVHNRTVIIIAH 538
Cdd:PLN03073 335 PEMQV----KATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYL--LKWPKTFIVVSH 399
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
474-550 |
9.42e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 45.59 E-value: 9.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 474 PMGEMGGQLSGGERQRISIARALL---KNAPVVILDEPTAAL---DIESELAVQKAIDNLVHnrTVIIIAHRLSTIAGAG 547
Cdd:PRK00635 802 PLGRPLSSLSGGEIQRLKLAYELLapsKKPTLYVLDEPTTGLhthDIKALIYVLQSLTHQGH--TVVIIEHNMHVVKVAD 879
|
...
gi 1805558896 548 NIL 550
Cdd:PRK00635 880 YVL 882
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
461-539 |
1.18e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 45.35 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 461 LEFISRLPQGWLTPMGemggQLSGGERQRISIA--RALLKN--APVVILDEPTAALDIESelaVQKaIDNLVHNRT---- 532
Cdd:pfam02463 1061 IEISARPPGKGVKNLD----LLSGGEKTLVALAliFAIQKYkpAPFYLLDEIDAALDDQN---VSR-VANLLKELSknaq 1132
|
....*..
gi 1805558896 533 VIIIAHR 539
Cdd:pfam02463 1133 FIVISLR 1139
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
33-212 |
1.28e-04 |
|
ABC transporter transmembrane region; This family represents a unit of six transmembrane helices. Many members of the ABC transporter family (pfam00005) have two such regions.
Pssm-ID: 459896 [Multi-domain] Cd Length: 274 Bit Score: 44.17 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 33 SMLALLLAAFMQGIAFACLYPIIDALLRGDAP---QLLNWAMAFSVAAIVTLVLRWygLGFEYRGHLAQ-ATHELRLRLG 108
Cdd:pfam00664 4 AILLAILSGAISPAFPLVLGRILDVLLPDGDPetqALNVYSLALLLLGLAQFILSF--LQSYLLNHTGErLSRRLRRKLF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 109 EQLRRVPLEKLQRGRAGEMNALLLGSVDENLNYVIAIANILLLTIVTPLTASLATLWIDWRLGLVMLLIFPLLVPFYYWR 188
Cdd:pfam00664 82 KKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAVF 161
|
170 180
....*....|....*....|....
gi 1805558896 189 RPAMRRQMQTLGEAHQRLSGDIVE 212
Cdd:pfam00664 162 AKILRKLSRKEQKAVAKASSVAEE 185
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
33-321 |
1.31e-04 |
|
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm288) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349991 [Multi-domain] Cd Length: 298 Bit Score: 44.32 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 33 SMLALLLAAFMQGIAFACLYPIIDALLRGDAPQLLNWAMAFSVAAIVTLVLRWyglgFEYR--GHLAQ-ATHELRLRLGE 109
Cdd:cd18547 11 STLLSVLGPYLLGKAIDLIIEGLGGGGGVDFSGLLRILLLLLGLYLLSALFSY----LQNRlmARVSQrTVYDLRKDLFE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 110 QLRRVPLEKLQRGRAGEMnalllgsvdenLNYVI----AIANILLLTIVTpLTASLAT--------LWIDWRLGLVMLLI 177
Cdd:cd18547 87 KLQRLPLSYFDTHSHGDI-----------MSRVTndvdNISQALSQSLTQ-LISSILTivgtlimmLYISPLLTLIVLVT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 178 FPLLVPFYYWR----RPAMRRQMQTLGEahqrLSGDIVEFAQGMMVLRTCGsdadKSRALLAHFNAL-ENLQTRTHR-QG 251
Cdd:cd18547 155 VPLSLLVTKFIakrsQKYFRKQQKALGE----LNGYIEEMISGQKVVKAFN----REEEAIEEFDEInEELYKASFKaQF 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1805558896 252 AGATM--LIASVVELGLQVVVLSGIVWVVTGTLNLAFLIAAVAMIMRFAEPMAMFIS-YTSVVELIASAlQRI 321
Cdd:cd18547 227 YSGLLmpIMNFINNLGYVLVAVVGGLLVINGALTVGVIQAFLQYSRQFSQPINQISQqINSLQSALAGA-ERV 298
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
455-571 |
1.37e-04 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 44.34 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 455 ARAAQCLEFISRLPQGwltpmGEMGGQLSGGERQRISIARALLKNAPVVILDEPTAALDIESELAVQKAIDNLVHNRTVI 534
Cdd:NF000106 123 ARADELLERFSLTEAA-----GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATV 197
|
90 100 110
....*....|....*....|....*....|....*....
gi 1805558896 535 IIAHRLSTIAG--AGNILVIEEGQVVEQGTHAQLLSHHG 571
Cdd:NF000106 198 LLTTQYMEEAEqlAHELTVIDRGRVIADGKVDELKTKVG 236
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
358-557 |
1.52e-04 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 44.66 E-value: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 358 GHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLTPEQLNSLISVVF----QDVWLFDD 433
Cdd:PRK15439 276 GEGFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARGLVYLpedrQSSGLYLD 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 434 --------TLLAN-----IRIARPQAtrqeVEEAARAAQCLEFiSRLPQGWLTpmgemggqLSGGERQRISIARALLKNA 500
Cdd:PRK15439 356 aplawnvcALTHNrrgfwIKPARENA----VLERYRRALNIKF-NHAEQAART--------LSGGNQQKVLIAKCLEASP 422
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1805558896 501 PVVILDEPTAALDIESELAVQKAIDNLV-HNRTVIIIAHRLSTIAG-AGNILVIEEGQV 557
Cdd:PRK15439 423 QLLIVDEPTRGVDVSARNDIYQLIRSIAaQNVAVLFISSDLEEIEQmADRVLVMHQGEI 481
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
482-571 |
2.96e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 43.73 E-value: 2.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 482 LSGGERQRISIARALLKNAPVVILDEPTAALDIESELAVQKAIDNlvHNRTVIIIAH-R--LSTIagAGNILVIEEGQVV 558
Cdd:PRK15064 439 LSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALEK--YEGTLIFVSHdRefVSSL--ATRIIEITPDGVV 514
|
90
....*....|....
gi 1805558896 559 E-QGTHAQLLSHHG 571
Cdd:PRK15064 515 DfSGTYEEYLRSQG 528
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
361-561 |
3.78e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 43.56 E-value: 3.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 361 LNHVSLTFPAASMSALVGASGAGKTTVTKLLM----RYADPQQGQISIGGVDIRRLTPEQLNSLISVVFQDVWL----FD 432
Cdd:TIGR00956 77 LKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDGITPEEIKKHYRGDVVYNAETDVHFphltVG 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 433 DTLLANIRIARPQATRQEVEEAARAAQCLEFISR---LPQGWLTPMG-EMGGQLSGGERQRISIARALLKNAPVVILDEP 508
Cdd:TIGR00956 157 ETLDFAARCKTPQNRPDGVSREEYAKHIADVYMAtygLSHTRNTKVGnDFVRGVSGGERKRVSIAEASLGGAKIQCWDNA 236
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1805558896 509 TAALDIESELAVQKAIDNLVH--NRTVIIIAHRLSTIAGA--GNILVIEEGQVVEQG 561
Cdd:TIGR00956 237 TRGLDSATALEFIRALKTSANilDTTPLVAIYQCSQDAYElfDKVIVLYEGYQIYFG 293
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
466-544 |
3.86e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 43.46 E-value: 3.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 466 RLPQGWLTPMGeMGGQ--------LSGGERQRISIARALLKNAPVVILDEPTAALDIESELAVQKAIDNLV-HNRTVII- 535
Cdd:PRK10938 379 KLAQQWLDILG-IDKRtadapfhsLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLIsEGETQLLf 457
|
90 100
....*....|....*....|
gi 1805558896 536 -----------IAHRLSTIA 544
Cdd:PRK10938 458 vshhaedapacITHRLEFVP 477
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
482-541 |
5.17e-04 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 43.20 E-value: 5.17e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 482 LSGGERQRISIARALLKNAPVVILDEPTAALDIESELAVQKAIDNLvhNRTVIIIAHRLS 541
Cdd:TIGR00954 583 LSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREF--GITLFSVSHRKS 640
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
482-538 |
8.94e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 42.20 E-value: 8.94e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1805558896 482 LSGGERQ------RISIARALLKNAPVVILDEPTAALD----------IESELAVQKAIDNlvhnrtVIIIAH 538
Cdd:PRK01156 802 LSGGEKTavafalRVAVAQFLNNDKSLLIMDEPTAFLDedrrtnlkdiIEYSLKDSSDIPQ------VIMISH 868
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
483-538 |
1.25e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 41.69 E-value: 1.25e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1805558896 483 SGGERQRISIARALLKNAPVVILDEPTAALDIESELAVQKAIDNlvHNRTVIIIAH 538
Cdd:PRK10636 151 SGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKS--YQGTLILISH 204
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
482-516 |
1.39e-03 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 41.47 E-value: 1.39e-03
10 20 30
....*....|....*....|....*....|....*
gi 1805558896 482 LSGGERQRISIARALLKNAPVVILDEPTAALDIES 516
Cdd:PRK11147 157 LSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIET 191
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
482-557 |
1.94e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 41.38 E-value: 1.94e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1805558896 482 LSGGERQRISIARALLKNAPVVILDEPTAALDIEselAVQKAIDNLV-HNRTVIIIAHRLSTIAGAGNIL-VIEEGQV 557
Cdd:PLN03073 628 LSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLD---AVEALIQGLVlFQGGVLMVSHDEHLISGSVDELwVVSEGKV 702
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
102-182 |
3.47e-03 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350020 [Multi-domain] Cd Length: 289 Bit Score: 39.77 E-value: 3.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 102 ELRLRLGEQLRRVPLEKLQRGRAGEMNALLLGSVDENLNYVIAIANILLLTIVTPLTASLATLWIDWRLGLVMLLIFPLL 181
Cdd:cd18576 70 DLRKDLYRHLQRLPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVV 149
|
.
gi 1805558896 182 V 182
Cdd:cd18576 150 V 150
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
480-559 |
3.64e-03 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 40.15 E-value: 3.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 480 GQLSGGERQRISIARALLKNAPVVILDEPTAALDIESELAVQKAIDNLVHN-RTVIIIAHRLSTI-AGAGNILVIEEGQV 557
Cdd:PRK09700 408 TELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDgKVILMVSSELPEIiTVCDRIAVFCEGRL 487
|
..
gi 1805558896 558 VE 559
Cdd:PRK09700 488 TQ 489
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
468-539 |
5.21e-03 |
|
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213239 [Multi-domain] Cd Length: 243 Bit Score: 38.78 E-value: 5.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 468 PQGWLTPMGEMGG-------QLSGGERQRISIAR--ALLK--NAPVVILDEPTAALDIESELAVQKAIDNLVHNRTVIII 536
Cdd:cd03272 138 PQGKINSLTNMKQdeqqemqQLSGGQKSLVALALifAIQKcdPAPFYLFDEIDAALDAQYRTAVANMIKELSDGAQFITT 217
|
...
gi 1805558896 537 AHR 539
Cdd:cd03272 218 TFR 220
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
34-221 |
7.84e-03 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This group includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins.
Pssm-ID: 350001 [Multi-domain] Cd Length: 289 Bit Score: 38.70 E-value: 7.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 34 MLALLLAAFMQGIAFACLYPIIDALLRGDAPQLLNW-AMAFSVAAIVTLVLRW-YGLGFEYRGHLAQAthELRLRLGEQL 111
Cdd:cd18557 2 LLFLLISSAAQLLLPYLIGRLIDTIIKGGDLDVLNElALILLAIYLLQSVFTFvRYYLFNIAGERIVA--RLRRDLFSSL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805558896 112 RRVPLEKLQRGRAGEMNALLLGSVDE-----NLNYVIAIANILLLTIVTPLTaslatLWIDWRLGLVMLLIFPLL--VPF 184
Cdd:cd18557 80 LRQEIAFFDKHKTGELTSRLSSDTSVlqsavTDNLSQLLRNILQVIGGLIIL-----FILSWKLTLVLLLVIPLLliASK 154
|
170 180 190
....*....|....*....|....*....|....*..
gi 1805558896 185 YYWRRpaMRRQMQTLGEAHQRLSGDIVEFAQGMMVLR 221
Cdd:cd18557 155 IYGRY--IRKLSKEVQDALAKAGQVAEESLSNIRTVR 189
|
|
| ABC_SMC2_euk |
cd03273 |
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ... |
469-514 |
9.45e-03 |
|
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213240 [Multi-domain] Cd Length: 251 Bit Score: 38.05 E-value: 9.45e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1805558896 469 QGWLTPMGEMGG-------QLSGGERQRI--SIARALL--KNAPVVILDEPTAALDI 514
Cdd:cd03273 147 QGRITKVLNMGGvwkesltELSGGQRSLValSLILALLlfKPAPMYILDEVDAALDL 203
|
|
| |
